Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we ide...
Ausführliche Beschreibung
Autor*in: |
Ticu, Cristina [verfasserIn] Nechifor, Roxana [verfasserIn] Nguyen, Boray [verfasserIn] Desrosiers, Melanie [verfasserIn] Wilson, Kevin S [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2009 |
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Schlagwörter: |
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Anmerkung: |
© European Molecular Biology Organization 2009 |
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Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 28(2009), 14 vom: 18. Juni, Seite 2053-2065 |
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Übergeordnetes Werk: |
volume:28 ; year:2009 ; number:14 ; day:18 ; month:06 ; pages:2053-2065 |
Links: |
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DOI / URN: |
10.1038/emboj.2009.169 |
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Katalog-ID: |
SPR057861366 |
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100 | 1 | |a Ticu, Cristina |e verfasserin |4 aut | |
245 | 1 | 0 | |a Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
264 | 1 | |c 2009 | |
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520 | |a Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. | ||
650 | 4 | |a elongation factor |7 (dpeaa)DE-He213 | |
650 | 4 | |a GTP hydrolysis |7 (dpeaa)DE-He213 | |
650 | 4 | |a ribosome |7 (dpeaa)DE-He213 | |
650 | 4 | |a translation |7 (dpeaa)DE-He213 | |
700 | 1 | |a Nechifor, Roxana |e verfasserin |4 aut | |
700 | 1 | |a Nguyen, Boray |e verfasserin |4 aut | |
700 | 1 | |a Desrosiers, Melanie |e verfasserin |4 aut | |
700 | 1 | |a Wilson, Kevin S |e verfasserin |4 aut | |
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912 | |a GBV_ILN_120 | ||
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912 | |a GBV_ILN_150 | ||
912 | |a GBV_ILN_151 | ||
912 | |a GBV_ILN_161 | ||
912 | |a GBV_ILN_168 | ||
912 | |a GBV_ILN_170 | ||
912 | |a GBV_ILN_171 | ||
912 | |a GBV_ILN_187 | ||
912 | |a GBV_ILN_213 | ||
912 | |a GBV_ILN_224 | ||
912 | |a GBV_ILN_230 | ||
912 | |a GBV_ILN_252 | ||
912 | |a GBV_ILN_266 | ||
912 | |a GBV_ILN_285 | ||
912 | |a GBV_ILN_293 | ||
912 | |a GBV_ILN_602 | ||
912 | |a GBV_ILN_636 | ||
912 | |a GBV_ILN_702 | ||
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912 | |a GBV_ILN_2005 | ||
912 | |a GBV_ILN_2006 | ||
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912 | |a GBV_ILN_2015 | ||
912 | |a GBV_ILN_2018 | ||
912 | |a GBV_ILN_2020 | ||
912 | |a GBV_ILN_2021 | ||
912 | |a GBV_ILN_2025 | ||
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 | ||
912 | |a GBV_ILN_2044 | ||
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 | ||
912 | |a GBV_ILN_2143 | ||
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912 | |a GBV_ILN_2147 | ||
912 | |a GBV_ILN_2148 | ||
912 | |a GBV_ILN_2152 | ||
912 | |a GBV_ILN_2153 | ||
912 | |a GBV_ILN_2188 | ||
912 | |a GBV_ILN_2190 | ||
912 | |a GBV_ILN_2232 | ||
912 | |a GBV_ILN_2336 | ||
912 | |a GBV_ILN_2470 | ||
912 | |a GBV_ILN_2472 | ||
912 | |a GBV_ILN_2507 | ||
912 | |a GBV_ILN_2522 | ||
912 | |a GBV_ILN_2548 | ||
912 | |a GBV_ILN_4012 | ||
912 | |a GBV_ILN_4029 | ||
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912 | |a GBV_ILN_4037 | ||
912 | |a GBV_ILN_4046 | ||
912 | |a GBV_ILN_4112 | ||
912 | |a GBV_ILN_4125 | ||
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912 | |a GBV_ILN_4242 | ||
912 | |a GBV_ILN_4246 | ||
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2009 |
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10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 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_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_4313 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_4700 AR 28 2009 14 18 06 2053-2065 |
spelling |
10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 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_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_4313 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_4700 AR 28 2009 14 18 06 2053-2065 |
allfields_unstemmed |
10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 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_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_4313 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_4700 AR 28 2009 14 18 06 2053-2065 |
allfieldsGer |
10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 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_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_4313 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_4700 AR 28 2009 14 18 06 2053-2065 |
allfieldsSound |
10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 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_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_4313 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_4700 AR 28 2009 14 18 06 2053-2065 |
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Ticu, Cristina @@aut@@ Nechifor, Roxana @@aut@@ Nguyen, Boray @@aut@@ Desrosiers, Melanie @@aut@@ Wilson, Kevin S @@aut@@ |
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Ticu, Cristina |
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Ticu, Cristina misc elongation factor misc GTP hydrolysis misc ribosome misc translation Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
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Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 |
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Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
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Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
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Ticu, Cristina Nechifor, Roxana Nguyen, Boray Desrosiers, Melanie Wilson, Kevin S |
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conformational changes in switch i of ef‐g drive its directional cycling on and off the ribosome |
title_auth |
Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
abstract |
Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009 |
abstractGer |
Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009 |
abstract_unstemmed |
Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009 |
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Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome |
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https://dx.doi.org/10.1038/emboj.2009.169 |
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Nechifor, Roxana Nguyen, Boray Desrosiers, Melanie Wilson, Kevin S |
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