The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadeny...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Jaggi, Rene [verfasserIn] van Heeswijk, Wally C. [verfasserIn] Westerhoff, Hans V. [verfasserIn] Ollis, David L. [verfasserIn] Vasudevan, Subhash G. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1997 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 1997 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 16(1997), 18 vom: 15. Sept., Seite 5562-5571 |
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| Übergeordnetes Werk: |
volume:16 ; year:1997 ; number:18 ; day:15 ; month:09 ; pages:5562-5571 |
| Links: |
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| DOI / URN: |
10.1093/emboj/16.18.5562 |
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| Katalog-ID: |
SPR057942870 |
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| 100 | 1 | |a Jaggi, Rene |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
| 264 | 1 | |c 1997 | |
| 336 | |a Text |b txt |2 rdacontent | ||
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| 500 | |a © European Molecular Biology Organization 1997 | ||
| 520 | |a Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. | ||
| 650 | 4 | |a adenylyl transferase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a flexible linker |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a intramolecular signal transduction |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a nucleotidyl transferase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a PII protein |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a van Heeswijk, Wally C. |e verfasserin |4 aut | |
| 700 | 1 | |a Westerhoff, Hans V. |e verfasserin |4 aut | |
| 700 | 1 | |a Ollis, David L. |e verfasserin |4 aut | |
| 700 | 1 | |a Vasudevan, Subhash G. |e verfasserin |4 aut | |
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| 912 | |a GBV_ILN_2021 | ||
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| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
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| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
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| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
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| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
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| 912 | |a GBV_ILN_2470 | ||
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| 912 | |a GBV_ILN_4125 | ||
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| 912 | |a GBV_ILN_4155 | ||
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| 912 | |a GBV_ILN_4249 | ||
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| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4311 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4314 | ||
| 912 | |a GBV_ILN_4318 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
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| 912 | |a GBV_ILN_4328 | ||
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| 952 | |d 16 |j 1997 |e 18 |b 15 |c 09 |h 5562-5571 | ||
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1997 |
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1997 |
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10.1093/emboj/16.18.5562 doi (DE-627)SPR057942870 (SPR)16.18.5562-e DE-627 ger DE-627 rakwb eng Jaggi, Rene verfasserin aut The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 van Heeswijk, Wally C. verfasserin aut Westerhoff, Hans V. verfasserin aut Ollis, David L. verfasserin aut Vasudevan, Subhash G. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 18 vom: 15. Sept., Seite 5562-5571 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 https://dx.doi.org/10.1093/emboj/16.18.5562 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 18 15 09 5562-5571 |
| spelling |
10.1093/emboj/16.18.5562 doi (DE-627)SPR057942870 (SPR)16.18.5562-e DE-627 ger DE-627 rakwb eng Jaggi, Rene verfasserin aut The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 van Heeswijk, Wally C. verfasserin aut Westerhoff, Hans V. verfasserin aut Ollis, David L. verfasserin aut Vasudevan, Subhash G. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 18 vom: 15. Sept., Seite 5562-5571 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 https://dx.doi.org/10.1093/emboj/16.18.5562 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 18 15 09 5562-5571 |
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10.1093/emboj/16.18.5562 doi (DE-627)SPR057942870 (SPR)16.18.5562-e DE-627 ger DE-627 rakwb eng Jaggi, Rene verfasserin aut The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 van Heeswijk, Wally C. verfasserin aut Westerhoff, Hans V. verfasserin aut Ollis, David L. verfasserin aut Vasudevan, Subhash G. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 18 vom: 15. Sept., Seite 5562-5571 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 https://dx.doi.org/10.1093/emboj/16.18.5562 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 18 15 09 5562-5571 |
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10.1093/emboj/16.18.5562 doi (DE-627)SPR057942870 (SPR)16.18.5562-e DE-627 ger DE-627 rakwb eng Jaggi, Rene verfasserin aut The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 van Heeswijk, Wally C. verfasserin aut Westerhoff, Hans V. verfasserin aut Ollis, David L. verfasserin aut Vasudevan, Subhash G. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 18 vom: 15. Sept., Seite 5562-5571 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 https://dx.doi.org/10.1093/emboj/16.18.5562 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 18 15 09 5562-5571 |
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10.1093/emboj/16.18.5562 doi (DE-627)SPR057942870 (SPR)16.18.5562-e DE-627 ger DE-627 rakwb eng Jaggi, Rene verfasserin aut The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 van Heeswijk, Wally C. verfasserin aut Westerhoff, Hans V. verfasserin aut Ollis, David L. verfasserin aut Vasudevan, Subhash G. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 18 vom: 15. Sept., Seite 5562-5571 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 https://dx.doi.org/10.1093/emboj/16.18.5562 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 18 15 09 5562-5571 |
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Enthalten in The EMBO Journal 16(1997), 18 vom: 15. Sept., Seite 5562-5571 volume:16 year:1997 number:18 day:15 month:09 pages:5562-5571 |
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adenylyl transferase flexible linker intramolecular signal transduction nucleotidyl transferase PII protein |
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The EMBO Journal |
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Jaggi, Rene @@aut@@ van Heeswijk, Wally C. @@aut@@ Westerhoff, Hans V. @@aut@@ Ollis, David L. @@aut@@ Vasudevan, Subhash G. @@aut@@ |
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This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. 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|
| author |
Jaggi, Rene |
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Jaggi, Rene misc adenylyl transferase misc flexible linker misc intramolecular signal transduction misc nucleotidyl transferase misc PII protein The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
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1460-2075 |
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The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction adenylyl transferase (dpeaa)DE-He213 flexible linker (dpeaa)DE-He213 intramolecular signal transduction (dpeaa)DE-He213 nucleotidyl transferase (dpeaa)DE-He213 PII protein (dpeaa)DE-He213 |
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misc adenylyl transferase misc flexible linker misc intramolecular signal transduction misc nucleotidyl transferase misc PII protein |
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misc adenylyl transferase misc flexible linker misc intramolecular signal transduction misc nucleotidyl transferase misc PII protein |
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misc adenylyl transferase misc flexible linker misc intramolecular signal transduction misc nucleotidyl transferase misc PII protein |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
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The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
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Jaggi, Rene |
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Jaggi, Rene van Heeswijk, Wally C. Westerhoff, Hans V. Ollis, David L. Vasudevan, Subhash G. |
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Elektronische Aufsätze |
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Jaggi, Rene |
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10.1093/emboj/16.18.5562 |
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the two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
| title_auth |
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
| abstract |
Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. © European Molecular Biology Organization 1997 |
| abstractGer |
Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. © European Molecular Biology Organization 1997 |
| abstract_unstemmed |
Abstract Adenylyl transferase (ATase) is the bifunctional effector enzyme in the nitrogen assimilation cascade that controls the activity of glutamine synthetase (GS) in Escherichia coli. This study addresses the question of whether the two antagonistic activities of ATase (adenylylation and deadenylylation) occur at the same or at different active sites. The 945 amino acid residue ATase has been truncated in two ways, so as to produce two homologous polypeptides corresponding to amino acids 1–423 (AT‐N) and 425–945 (AT‐C). We demonstrate that ATase has two active sites; AT‐N carries a deadenylylation activity and AT‐C carries an adenylylation activity. Glutamine activates the adenylylation reaction of the AT‐C domain, whereas α‐ketoglutarate activates the deadenylylation reaction catalysed by the AT‐N domain. With respect to the regulation by the nitrogen status monitor PII, however, the adenylylation domain appears to be dependent on the deadenylylation domain: the deadenylylation activity of AT‐N depends on PII‐UMP and is inhibited by PII. The adenylylation activity of AT‐C is independent of PII (or PII‐UMP), whereas in the intact enzyme PII is required for this activity. The implications of this intramolecular signal transduction for the prevention of futile cycling are discussed. © European Molecular Biology Organization 1997 |
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| title_short |
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction |
| url |
https://dx.doi.org/10.1093/emboj/16.18.5562 |
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van Heeswijk, Wally C. Westerhoff, Hans V. Ollis, David L. Vasudevan, Subhash G. |
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van Heeswijk, Wally C. Westerhoff, Hans V. Ollis, David L. Vasudevan, Subhash G. |
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10.1093/emboj/16.18.5562 |
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| score |
7.3980484 |