Cooperation and competition in mismatch repair: Very short-patch repair and methyl-directed mismatch repair in Escherichia coli

Molecular Microbiology

Volumn 44, Issue 6, 2002, Pages 1421-1428

  Bhagwat, Ashok S ^a   Lieb, Margaret ^b  

^a WAYNE STATE UNIVERSITY   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5 METHYLCYTOSINE; BACTERIAL PROTEIN; DNA BASE; ENDONUCLEASE; METHYL GROUP; PROTEIN MUTL; PROTEIN MUTS; UNCLASSIFIED DRUG; ADENINE; ADENOSINE TRIPHOSPHATASE; DEOXYRIBONUCLEASE; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; MUTL PROTEIN, E COLI; MUTS PROTEIN, E COLI; VSR ENDONUCLEASE;

BACTERIAL GROWTH; BASE MISPAIRING; BIOCHEMISTRY; CELL; CONTROLLED STUDY; DEAMINATION; DNA REPLICATION; ENTEROBACTERIACEAE; ESCHERICHIA COLI; LIFE CYCLE; MISMATCH REPAIR; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SHORT SURVEY; CHEMICAL STRUCTURE; CHEMISTRY; DNA METHYLATION; DNA REPAIR; GENETICS; METABOLISM; REVIEW;

ADENINE; ADENOSINETRIPHOSPHATASE; BASE PAIR MISMATCH; DNA METHYLATION; DNA REPAIR; DNA-BINDING PROTEINS; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; SUPPORT, U.S. GOV'T, P.H.S.; ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; MUTS DNA MISMATCH-BINDING PROTEIN;

BACTERIA (MICROORGANISMS); ENTEROBACTERIACEAE; ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036016788     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.02989.x     Document Type: Short Survey

References (50)

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3. Very short-patch repair in Escherichia coli requires the dam adenine methylase
4. Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism
5. Overexpression of vsr in Escherichia coli is mutagenic
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13. The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch
14. hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA
15. Mismatch repair protein MutL becomes limiting during stationary-phase mutation
16. Mismatch repair is diminished during stationary-phase mutation
17. PvuII endonuclease contains two calcium ions in active sites
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20. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair
21. The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch
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37. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
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