Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis
Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐strand...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Dekker, Job [verfasserIn] Kanellopoulos, Panagiotis N. [verfasserIn] Loonstra, Ate K. [verfasserIn] van Oosterhout, Joost A.W.M. [verfasserIn] Leonard, Kevin [verfasserIn] Tucker, Paul A. [verfasserIn] van der Vliet, Peter C. [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), 6 vom: 15. März, Seite 1455-1463 |
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| Übergeordnetes Werk: |
volume:16 ; year:1997 ; number:6 ; day:15 ; month:03 ; pages:1455-1463 |
| Links: |
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| DOI / URN: |
10.1093/emboj/16.6.1455 |
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| Katalog-ID: |
SPR05794413X |
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| 100 | 1 | |a Dekker, Job |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis |
| 264 | 1 | |c 1997 | |
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| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 500 | |a © European Molecular Biology Organization 1997 | ||
| 520 | |a Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. | ||
| 650 | 4 | |a adenovirus |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a DNA replication |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a DNA unwinding |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a helix‐destabilizing proteins |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Kanellopoulos, Panagiotis N. |e verfasserin |4 aut | |
| 700 | 1 | |a Loonstra, Ate K. |e verfasserin |4 aut | |
| 700 | 1 | |a van Oosterhout, Joost A.W.M. |e verfasserin |4 aut | |
| 700 | 1 | |a Leonard, Kevin |e verfasserin |4 aut | |
| 700 | 1 | |a Tucker, Paul A. |e verfasserin |4 aut | |
| 700 | 1 | |a van der Vliet, Peter C. |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The EMBO Journal |d Nature Publishing Group UK, 2023 |g 16(1997), 6 vom: 15. März, Seite 1455-1463 |w (DE-627)266022529 |w (DE-600)1467419-1 |x 1460-2075 |7 nnns |
| 773 | 1 | 8 | |g volume:16 |g year:1997 |g number:6 |g day:15 |g month:03 |g pages:1455-1463 |
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| 912 | |a GBV_ILN_2068 | ||
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| 912 | |a GBV_ILN_2093 | ||
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10.1093/emboj/16.6.1455 doi (DE-627)SPR05794413X (SPR)16.6.1455-e DE-627 ger DE-627 rakwb eng Dekker, Job verfasserin aut Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 Kanellopoulos, Panagiotis N. verfasserin aut Loonstra, Ate K. verfasserin aut van Oosterhout, Joost A.W.M. verfasserin aut Leonard, Kevin verfasserin aut Tucker, Paul A. verfasserin aut van der Vliet, Peter C. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 6 vom: 15. März, Seite 1455-1463 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 https://dx.doi.org/10.1093/emboj/16.6.1455 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 6 15 03 1455-1463 |
| spelling |
10.1093/emboj/16.6.1455 doi (DE-627)SPR05794413X (SPR)16.6.1455-e DE-627 ger DE-627 rakwb eng Dekker, Job verfasserin aut Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 Kanellopoulos, Panagiotis N. verfasserin aut Loonstra, Ate K. verfasserin aut van Oosterhout, Joost A.W.M. verfasserin aut Leonard, Kevin verfasserin aut Tucker, Paul A. verfasserin aut van der Vliet, Peter C. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 6 vom: 15. März, Seite 1455-1463 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 https://dx.doi.org/10.1093/emboj/16.6.1455 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 6 15 03 1455-1463 |
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10.1093/emboj/16.6.1455 doi (DE-627)SPR05794413X (SPR)16.6.1455-e DE-627 ger DE-627 rakwb eng Dekker, Job verfasserin aut Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 Kanellopoulos, Panagiotis N. verfasserin aut Loonstra, Ate K. verfasserin aut van Oosterhout, Joost A.W.M. verfasserin aut Leonard, Kevin verfasserin aut Tucker, Paul A. verfasserin aut van der Vliet, Peter C. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 6 vom: 15. März, Seite 1455-1463 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 https://dx.doi.org/10.1093/emboj/16.6.1455 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 6 15 03 1455-1463 |
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10.1093/emboj/16.6.1455 doi (DE-627)SPR05794413X (SPR)16.6.1455-e DE-627 ger DE-627 rakwb eng Dekker, Job verfasserin aut Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 Kanellopoulos, Panagiotis N. verfasserin aut Loonstra, Ate K. verfasserin aut van Oosterhout, Joost A.W.M. verfasserin aut Leonard, Kevin verfasserin aut Tucker, Paul A. verfasserin aut van der Vliet, Peter C. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 6 vom: 15. März, Seite 1455-1463 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 https://dx.doi.org/10.1093/emboj/16.6.1455 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 6 15 03 1455-1463 |
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10.1093/emboj/16.6.1455 doi (DE-627)SPR05794413X (SPR)16.6.1455-e DE-627 ger DE-627 rakwb eng Dekker, Job verfasserin aut Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 Kanellopoulos, Panagiotis N. verfasserin aut Loonstra, Ate K. verfasserin aut van Oosterhout, Joost A.W.M. verfasserin aut Leonard, Kevin verfasserin aut Tucker, Paul A. verfasserin aut van der Vliet, Peter C. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 6 vom: 15. März, Seite 1455-1463 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 https://dx.doi.org/10.1093/emboj/16.6.1455 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 6 15 03 1455-1463 |
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Enthalten in The EMBO Journal 16(1997), 6 vom: 15. März, Seite 1455-1463 volume:16 year:1997 number:6 day:15 month:03 pages:1455-1463 |
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adenovirus DNA replication DNA unwinding helix‐destabilizing proteins |
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Dekker, Job @@aut@@ Kanellopoulos, Panagiotis N. @@aut@@ Loonstra, Ate K. @@aut@@ van Oosterhout, Joost A.W.M. @@aut@@ Leonard, Kevin @@aut@@ Tucker, Paul A. @@aut@@ van der Vliet, Peter C. @@aut@@ |
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Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. 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Dekker, Job |
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Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis adenovirus (dpeaa)DE-He213 DNA replication (dpeaa)DE-He213 DNA unwinding (dpeaa)DE-He213 helix‐destabilizing proteins (dpeaa)DE-He213 |
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Dekker, Job Kanellopoulos, Panagiotis N. Loonstra, Ate K. van Oosterhout, Joost A.W.M. Leonard, Kevin Tucker, Paul A. van der Vliet, Peter C. |
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multimerization of the adenovirus dna‐binding protein is the driving force for atp‐independent dna unwinding during strand displacement synthesis |
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Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis |
| abstract |
Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. © European Molecular Biology Organization 1997 |
| abstractGer |
Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. © European Molecular Biology Organization 1997 |
| abstract_unstemmed |
Abstract In contrast to other replication systems, adenovirus DNA replication does not require a DNA helicase to unwind the double‐stranded template. Elongation is dependent on the adenovirus DNA‐binding protein (DBP) which has helix‐destabilizing properties. DBP binds cooperatively to single‐stranded DNA (ssDNA) in a non‐sequence‐specific manner. The crystal structure of DBP shows that the protein has a C‐terminal extension that hooks on to an adjacent monomer which results in the formation of long protein chains. We show that deletion of this C‐terminal arm results in a monomeric protein. The mutant binds with a greatly reduced affinity to ssDNA. The deletion mutant still stimulates initiation of DNA replication like the intact DBP. This shows that a high affinity of DBP for ssDNA is not required for initiation. On a single‐stranded template, elongation is also observed in the absence of DBP. Addition of DBP or the deletion mutant has no effect on elongation, although both proteins stimulate initiation on this template. Strand displacement synthesis on a double‐stranded template is only observed in the presence of DBP. The mutant, however, does not support elongation on a double‐stranded template. The unwinding activity of the mutant is highly reduced compared with intact DBP. These data suggest that protein chain formation by DBP and high affinity binding to the displaced strand drive the ATP‐independent unwinding of the template during adenovirus DNA replication. © European Molecular Biology Organization 1997 |
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| title_short |
Multimerization of the adenovirus DNA‐binding protein is the driving force for ATP‐independent DNA unwinding during strand displacement synthesis |
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https://dx.doi.org/10.1093/emboj/16.6.1455 |
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Kanellopoulos, Panagiotis N. Loonstra, Ate K. van Oosterhout, Joost A.W.M. Leonard, Kevin Tucker, Paul A. van der Vliet, Peter C. |
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Kanellopoulos, Panagiotis N. Loonstra, Ate K. van Oosterhout, Joost A.W.M. Leonard, Kevin Tucker, Paul A. van der Vliet, Peter C. |
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| score |
7.4018106 |