Document Detail


Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes.
MedLine Citation:
PMID:  22570477     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The single-stranded DNA (ssDNA)-binding protein from the radiation-resistant bacterium Deinococcus radiodurans (DrSSB) functions as a homodimer in which each monomer contains two oligonucleotide-binding (OB) domains. This arrangement is exceedingly rare among bacterial SSBs, which typically form homotetramers of single-OB domain subunits. To better understand how this unusual structure influences the DNA binding and biological functions of DrSSB in D. radiodurans radiation resistance, we have examined the structure of DrSSB in complex with ssDNA and the DNA damage-dependent cellular dynamics of DrSSB. The x-ray crystal structure of the DrSSB-ssDNA complex shows that ssDNA binds to surfaces of DrSSB that are analogous to those mapped in homotetrameric SSBs, although there are distinct contacts in DrSSB that mediate species-specific ssDNA binding. Observations by electron microscopy reveal two salt-dependent ssDNA-binding modes for DrSSB that strongly resemble those of the homotetrameric Escherichia coli SSB, further supporting a shared overall DNA binding mechanism between the two classes of bacterial SSBs. In vivo, DrSSB levels are heavily induced following exposure to ionizing radiation. This accumulation is accompanied by dramatic time-dependent DrSSB cellular dynamics in which a single nucleoid-centric focus of DrSSB is observed within 1 h of irradiation but is dispersed by 3 h after irradiation. These kinetics parallel those of D. radiodurans postirradiation genome reconstitution, suggesting that DrSSB dynamics could play important organizational roles in DNA repair.
Authors:
Nicholas P George; Khanh V Ngo; Sindhu Chitteni-Pattu; Cédric A Norais; John R Battista; Michael M Cox; James L Keck
Related Documents :
22336087 - The increased incidence of malignant melanoma in obese individuals is due to impaired m...
9407637 - Collaborative study to assess the suitability of a proposed working reagent for human p...
24675077 - The role of the human psoralen 4 (hpso4) complex in replication stress and homologous r...
9215657 - Increased expression of interleukin-2 receptor alpha on peripheral blood mononuclear ce...
24361487 - Dna strand generation for dna computing by using a multi-objective differential evoluti...
2157057 - Mutation of a consensus purine nucleotide binding site in the adeno-associated virus re...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-05-07
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  287     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-06-25     Completed Date:  2012-09-20     Revised Date:  2013-06-25    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  22123-32     Citation Subset:  IM    
Affiliation:
Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/3UDG
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Crystallography, X-Ray / methods
DNA Damage
DNA, Single-Stranded / genetics*
DNA-Binding Proteins / chemistry*,  metabolism
Deinococcus / metabolism*
Escherichia coli / metabolism
Kinetics
Microscopy, Electron / methods
Microscopy, Fluorescence / methods
Models, Molecular
Oligonucleotides / chemistry
Protein Binding
Protein Structure, Tertiary
Radiation, Ionizing
Recombination, Genetic
Salts / chemistry
Grant Support
ID/Acronym/Agency:
GM068061/GM/NIGMS NIH HHS; GM32335/GM/NIGMS NIH HHS; R01 GM032335/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/DNA, Single-Stranded; 0/DNA-Binding Proteins; 0/Oligonucleotides; 0/Salts
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Okazaki fragment processing-independent role for human Dna2 enzyme during DNA replication.
Next Document:  Proximal recognition sites facilitate intrasite hopping by DNA adenine methyltransferase: mechanisti...