Escherichia coli RadD Protein Functionally Interacts with the Single-stranded DNA-binding Protein

被引：29

作者：

Chen, Stefanie H. ^{[1
]}

Byrne-Nash, Rose T. ^{[1
]}

Cox, Michael M. ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Biochem, 433 Babcock Dr,Rm 337, Madison, WI 53706 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2016年 / 291卷 / 39期

基金：

美国国家卫生研究院;

关键词：

ATPase; DNA repair; protein-DNA interaction; protein-protein interaction; radiation biology; SSB; helicase; COMPLEX-FORMATION; SSB; REPLICATION; HELICASE; PURIFICATION; MECHANISM; RADIATION; RESIDUES; SUBUNITS; REPAIR;

D O I：

10.1074/jbc.M116.736223

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The bacterial single-stranded DNA binding protein (SSB) acts as an organizer of DNA repair complexes. The radD gene was recently identified as having an unspecified role in repair of radiation damage and, more specifically, DNA double-strand breaks. Purified RadD protein displays a DNA-independent ATPase activity. However, ATP hydrolytic rates are stimulated by SSB through its C terminus. The RadD and SSB proteins also directly interact in vivo in a yeast two-hybrid assay and in vitro through ammonium sulfate co-precipitation. Therefore, it is likely that the repair function of RadD is mediated through interaction with SSB at the site of damage.

引用

页码：20779 / 20786

页数：8

共 28 条

[1] Multiple C-Terminal Tails within a Single E. coli SSB Homotetramer Coordinate DNA Replication and Repair [J].

Antony, Edwin ;

Weiland, Elizabeth ;

Yuan, Quan ;

Manhart, Carol M. ;

Binh Nguyen ;

Kozlov, Alexander G. ;

McHenry, Charles S. ;

Lohman, Timothy M. .

JOURNAL OF MOLECULAR BIOLOGY, 2013, 425 (23) :4802-4819

[2] Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding [J].

Aramaki, Takahiko ;

Abe, Yoshito ;

Furutani, Kaori ;

Katayama, Tsutomu ;

Ueda, Tadashi .

JOURNAL OF BIOCHEMISTRY, 2015, 157 (06) :529-537

[3] Identification of genes involved in low aminoglycoside-induced SOS response in Vibrio cholerae: a role for transcription stalling and Mfd helicase [J].

Baharoglu, Zeynep ;

Babosan, Anamaria ;

Mazel, Didier .

NUCLEIC ACIDS RESEARCH, 2014, 42 (04) :2366-2379

[4] Role for radA/sms in recombination intermediate processing in Escherichia coli [J].

Beam, CE ;

Saveson, CJ ;

Lovett, ST .

JOURNAL OF BACTERIOLOGY, 2002, 184 (24) :6836-6844

[5] Escherichia coli Genes and Pathways Involved in Surviving Extreme Exposure to Ionizing Radiation [J].

Byrne, Rose T. ;

Chen, Stefanie H. ;

Wood, Elizabeth A. ;

Cabot, Eric L. ;

Cox, Michael M. .

JOURNAL OF BACTERIOLOGY, 2014, 196 (20) :3534-3545

[6] PriA helicase and SSB interact physically and functionally [J].

Cadman, CJ ;

McGlynn, P .

NUCLEIC ACIDS RESEARCH, 2004, 32 (21) :6378-6387

[7] Escherichia coli radD (yejH) gene: a novel function involved in radiation resistance and double-strand break repair [J].

Chen, Stefanie H. ;

Byrne, Rose T. ;

Wood, Elizabeth A. ;

Cox, Michael M. .

MOLECULAR MICROBIOLOGY, 2015, 95 (05) :754-768

[8] Recombinational branch migration by the RadA/Sms paralog of RecA in Escherichia coli [J].

Cooper, Deani L. ;

Lovett, Susan T. .

ELIFE, 2016, 5

[9] Interaction between Escherichia coli DNA polymerase IV and single-stranded DNA-binding protein is required for DNA synthesis on SSB-coated DNA [J].

Furukohri, Asako ;

Nishikawa, Yoshito ;

Akiyama, Masahiro Tatsumi ;

Maki, Hisaji .

NUCLEIC ACIDS RESEARCH, 2012, 40 (13) :6039-6048

[10] The χψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template [J].

Glover, BP ;

McHenry, CS .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (36) :23476-23484

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