Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4

Iain D. Kerr, Sivashankar Sivakolundu, Zhenmei Li, Jeffrey C. Buchsbaum, Luke A. Knox, Richard Kriwacki, Stephen W. White

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3′-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7 Å and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.

Original languageEnglish (US)
Pages (from-to)34392-34400
Number of pages9
JournalJournal of Biological Chemistry
Volume282
Issue number47
DOIs
StatePublished - Nov 23 2007
Externally publishedYes

Fingerprint

Bacteriophage T4
Bacteriophages
Nucleic Acids
Nuclear magnetic resonance
Genetic Recombination
Substrates
Genes
RecQ Helicases
Recombinases
Escherichia coli
Open Reading Frames
Sequence Analysis
Proteins
Repair
Crystal structure
Genome

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kerr, I. D., Sivakolundu, S., Li, Z., Buchsbaum, J. C., Knox, L. A., Kriwacki, R., & White, S. W. (2007). Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. Journal of Biological Chemistry, 282(47), 34392-34400. https://doi.org/10.1074/jbc.M705900200

Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. / Kerr, Iain D.; Sivakolundu, Sivashankar; Li, Zhenmei; Buchsbaum, Jeffrey C.; Knox, Luke A.; Kriwacki, Richard; White, Stephen W.

In: Journal of Biological Chemistry, Vol. 282, No. 47, 23.11.2007, p. 34392-34400.

Research output: Contribution to journalArticle

Kerr, ID, Sivakolundu, S, Li, Z, Buchsbaum, JC, Knox, LA, Kriwacki, R & White, SW 2007, 'Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4', Journal of Biological Chemistry, vol. 282, no. 47, pp. 34392-34400. https://doi.org/10.1074/jbc.M705900200
Kerr ID, Sivakolundu S, Li Z, Buchsbaum JC, Knox LA, Kriwacki R et al. Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. Journal of Biological Chemistry. 2007 Nov 23;282(47):34392-34400. https://doi.org/10.1074/jbc.M705900200
Kerr, Iain D. ; Sivakolundu, Sivashankar ; Li, Zhenmei ; Buchsbaum, Jeffrey C. ; Knox, Luke A. ; Kriwacki, Richard ; White, Stephen W. / Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 47. pp. 34392-34400.
@article{2090a8f147f74ebb909340cacc125abb,
title = "Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4",
abstract = "The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3′-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7 {\AA} and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.",
author = "Kerr, {Iain D.} and Sivashankar Sivakolundu and Zhenmei Li and Buchsbaum, {Jeffrey C.} and Knox, {Luke A.} and Richard Kriwacki and White, {Stephen W.}",
year = "2007",
month = "11",
day = "23",
doi = "10.1074/jbc.M705900200",
language = "English (US)",
volume = "282",
pages = "34392--34400",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "47",

}

TY - JOUR

T1 - Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4

AU - Kerr, Iain D.

AU - Sivakolundu, Sivashankar

AU - Li, Zhenmei

AU - Buchsbaum, Jeffrey C.

AU - Knox, Luke A.

AU - Kriwacki, Richard

AU - White, Stephen W.

PY - 2007/11/23

Y1 - 2007/11/23

N2 - The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3′-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7 Å and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.

AB - The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3′-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7 Å and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.

UR - http://www.scopus.com/inward/record.url?scp=36348952191&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36348952191&partnerID=8YFLogxK

U2 - 10.1074/jbc.M705900200

DO - 10.1074/jbc.M705900200

M3 - Article

C2 - 17878153

AN - SCOPUS:36348952191

VL - 282

SP - 34392

EP - 34400

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 47

ER -