mutS:Quickview: Difference between revisions
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MutS also functions as an ATPase, providing energy for the MMR pathway. After binding to the mismatch, a hemi-methylated dGATC site is located and cleaved by other MMR enzymes. This dGATC binding site is either in the 3' or 5' direction from the mismatch. The entire MMR process is a highly conserved pathway with great similarities between the human pathway and ''E. coli'' pathway. The human homolog, MutSα, acts virtually the same as the ''E. coli'' form of the protein.<ref name='PMID:18157157'/> | MutS also functions as an ATPase, providing energy for the MMR pathway. After binding to the mismatch, a hemi-methylated dGATC site is located and cleaved by other MMR enzymes. This dGATC binding site is either in the 3' or 5' direction from the mismatch. The entire MMR process is a highly conserved pathway with great similarities between the human pathway and ''E. coli'' pathway. The human homolog, MutSα, acts virtually the same as the ''E. coli'' form of the protein.<ref name='PMID:18157157'/> | ||
MutS has weak ATPase activity and may be involved in recognizing the DNA mismatch. MutS C-terminus dimerization, not tetramerization, is required for mismatch repair | MutS has weak ATPase activity and may be involved in recognizing the DNA mismatch. MutS C-terminus dimerization, not tetramerization, is required for mismatch repair. <ref name='PMID:17426027'/> <ref name='LIB:EcoGene'/> | ||
Revision as of 22:04, 15 April 2010
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
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| Standard Name |
mutS |
|---|---|
| Gene Synonym(s) |
ECK2728, b2733, JW2703, fdv, ant, plm[1] |
| Product Desc. |
Component of MutHLS complex, methyl-directed mismatch repair[2][3] Methyl-directed mismatch repair protein; dimeric/tetrameric[4] |
| Product Synonyms(s) |
methyl-directed mismatch repair protein[1], B2733[2][1], Plm[2][1], Ant[2][1], Fdv[2][1], MutS[2][1] |
| Function from GO |
<GO_nr /> |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity | |
| Quick Links | |
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Notes
MutS, also known as the "mismatch recognition" enzyme, is essential for the DNA mismatch repair (MMR) biological pathway. It recognizes base-base mismatches and small nucleotide insertion/deletion mispairs generated during DNA synthesis or damage caused by various agents. After recognizing the mismatches, MutS binds to the mismatch as a homodimer. Although the MutS binding site is sequence-wise identical, the mismatch and MutS are structurally and functionally different, so it is virtually a heterodimer.
MutS also functions as an ATPase, providing energy for the MMR pathway. After binding to the mismatch, a hemi-methylated dGATC site is located and cleaved by other MMR enzymes. This dGATC binding site is either in the 3' or 5' direction from the mismatch. The entire MMR process is a highly conserved pathway with great similarities between the human pathway and E. coli pathway. The human homolog, MutSα, acts virtually the same as the E. coli form of the protein.[5]
MutS has weak ATPase activity and may be involved in recognizing the DNA mismatch. MutS C-terminus dimerization, not tetramerization, is required for mismatch repair. [6] [4]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Li, GM (2008) Mechanisms and functions of DNA mismatch repair. Cell Res. 18 85-98 PubMed
- ↑ Mendillo, ML et al. (2007) Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo. J. Biol. Chem. 282 16345-54 PubMed