The Escherichia coli fdv gene probably encodes mutS and is located at minute 58.8 adjacent to the hyc-hyp gene cluster

Schlensog, V; Böck, August

doi:10.1128/jb.173.23.7414-7415.1991

Cited by 20 publications

(10 citation statements)

References 13 publications

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“…ophimuritlm, Strep. pneumoniae and Axotobacter vinelandii, confirmed the functional similarities. The MutS and HexA proteins are highly similar, and so are MutL and HexB (Connoly & Winkler, 1992;Haber e t al., 1988;Le e t a/., 1993;Mankovich e t al., 1989;Prudhomme e t al., 1989Prudhomme e t al., , 1991Priebe e t al., 1988 ;Schlensong & Boeck, 1991). Negative complementation conferred by the expression in E. coli of the Strep, pneumonzae HexA function confirmed their common evolutionary origin (Prudhomme e t al., 1991).…”

Section: Introductionmentioning

confidence: 79%

Bacillus subtilis mutS mutL operon: identification, nucleotide sequence and mutagenesis

Ginetti

Perego²,

Albertini³

et al. 1996

Microbiology

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Section: Introductionmentioning

confidence: 79%

Bacillus subtilis mutS mutL operon: identification, nucleotide sequence and mutagenesis

Ginetti

Perego²,

Albertini³

et al. 1996

Microbiology

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“…strain ADP1. Nucleotide sequencing revealed that the mutS ORF is 2,646 bp in length and is predicted to encode a 97-kDa product that possesses approximately 50% amino acid sequence identity to the MutS homolog from E. coli (43). Sequence analysis of about 3 kb of DNA on both sides of mutS disclosed six additional ORFs (Fig.…”

Section: Resultsmentioning

confidence: 99%

Functions of the Mismatch Repair Gene mutS from Acinetobacter sp. Strain ADP1

Young

Ornston

2001

J Bacteriol

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The genus Acinetobacter encompasses a heterogeneous group of bacteria that are ubiquitous in the natural environment due in part to their ability to adapt genetically to novel challenges. Acinetobacter sp. strain ADP1 (also known as strain BD413) is naturally transformable and takes up DNA from any source. Donor DNA can be integrated into the chromosome by recombination provided it possesses sufficient levels of nucleotide sequence identity to the recipient's DNA. In other bacteria, the requirement for sequence identity during recombination is partly due to the actions of the mismatch repair system, a key component of which, MutS, recognizes mismatched bases in heteroduplex DNA and, along with MutL, blocks strand exchange. We have cloned mutS from strain ADP1 and examined its roles in preventing recombination between divergent DNA and in the repair of spontaneous replication errors. Inactivation of mutS resulted in 3-to 17-fold increases in transformation efficiencies with donor sequences that were 8 to 20% divergent relative to the strain ADP1. Strains lacking MutS exhibited increased spontaneous mutation frequencies, and reversion assays demonstrated that MutS preferentially recognized transition mismatches while having little effect on the repair of transversion mismatches. Inactivation of mutS also abolished the marker-specific variations in transforming efficiency seen in mutS ؉ recipients where transition and frameshift alleles transformed at eightfold lower frequencies than transversions or large deletions. Comparison of the MutS homologs from five individual Acinetobacter strains with those of other gram-negative bacteria revealed that a number of unique indels are conserved among the Acinetobacter amino acid sequences.

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“…An expression plasmid for MutS800 was constructed by PCR amplification of the appropriate sequence of the MutS gene of plasmid pMS1 (25,28) followed by subcloning into a pT7-3 expression vector using EcoRI and BamHI endonuclease restriction sites. E. coli MutS and MutS800 proteins were purified as described (23) and stored as concentrated stocks in 50 mM KPO 4 , pH 7.4, 150 mM KCl, 1 mM 2-mercaptoethanol, and 50% (v/v) glycerol at Ϫ20°C.…”

Section: Methodsmentioning

confidence: 99%

Assembly and Molecular Activities of the MutS Tetramer

Bjornson¹,

Blackwell²,

Sage³

et al. 2003

Journal of Biological Chemistry

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Analytical equilibrium ultracentrifugation indicates that Escherichia coli MutS exists as an equilibrating mixture of dimers and tetramers. The association constant for the dimer-to-tetramer transition is 2.1 ؋ 10 7 M ؊1 , indicating that the protein would consist of both dimers and tetramers at physiological concentrations. The carboxyl terminus of MutS is required for tetramer assembly because a previously described 53-amino acid carboxyl-terminal truncation (MutS800) forms a limiting species of a dimer (Obmolova, G., Ban, C., Hsieh, P., and Yang, W. MutS homologs participate in multiple genetic stabilization pathways by virtue of their ability to recognize a spectrum of DNA lesions. Recognition of base pair mismatches by MutS homologs has been implicated in the rectification of DNA biosynthetic errors and in the dissolution of recombination events involving diverged sequences (1-5). Recognition of damaged base pairs by MutS homologs is also involved in the transcription-coupled repair of DNA damage (2, 4) and has been implicated in the activation of checkpoint and apoptotic responses to certain types of DNA damage in mammalian cells (6). Members of the MutS family can thus be viewed as molecular sentinels that respond to subtle variations in DNA structure or dynamics and then communicate presence of that lesion to downstream activities (1, 7-9).Events downstream of MutS recognition have been delineated for the Escherichia coli pathway responsible for correction of DNA biosynthetic errors, and this reaction has been reconstituted in vitro using near homogeneous components. Although a number of mechanistic details remain to be established, basic roles of the individual activities have been defined. MutS recruits MutL to the heteroduplex in a reaction requiring ATP (10 -12). Assembly of this ternary complex is sufficient to activate the latent endonuclease activity of MutH, which incises the unmethylated strand at a hemimethylated d(GATC) strand signal (13). In addition, this complex activates the unwinding activity of DNA helicase II, which loads at the MutH incision with an orientation bias so that helix unwinding proceeds toward the mismatch (14, 15). The unwound portion of the incised strand is hydrolyzed by a single-strand exonuclease. If unwinding proceeds from a strand break located 5Ј to the mispair, the displaced single strand is degraded by the 5Ј-to-3Ј hydrolytic activity of ExoVII or RecJ exonuclease (16,17). When helicase unwinding initiates at a nick 3Ј to the mismatch, the unwound strand is degraded by the 3Ј-to-5Ј activity of ExoI, ExoVII,. Excision terminates at a number of sites centered about 50 base pairs beyond the mismatch, the ensuing gap is repaired by DNA polymerase III holoenzyme in the presence of single-strand binding protein, and DNA ligase restores covalent integrity to the repaired strand (18,20).In addition to its mismatch recognition activity, bacterial MutS harbors a weak ATPase (21) that is stimulated by DNA (22). Because the rate-limiting step for ATP hydrolytic turnover is se...

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The Escherichia coli fdv gene probably encodes mutS and is located at minute 58.8 adjacent to the hyc-hyp gene cluster

Cited by 20 publications

References 13 publications

Bacillus subtilis mutS mutL operon: identification, nucleotide sequence and mutagenesis

Bacillus subtilis mutS mutL operon: identification, nucleotide sequence and mutagenesis

Functions of the Mismatch Repair Gene mutS from Acinetobacter sp. Strain ADP1

Assembly and Molecular Activities of the MutS Tetramer

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