4fmn
Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of NTG2Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of NTG2
Template:ABSTRACT PUBMED 23435383
FunctionFunction
[MLH1_YEAST] Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of different MutL heterodimers that form a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over.[1] [2] [3] [NTG2_YEAST] Excision repair N-glycosylase involved in the repair of DNA base damage in the nucleus. NTG2 can use dihydrothymine (poor substrate), urea, and uracil glycol are substrates. [PMS1_YEAST] Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates.[4] [5] [6]
About this StructureAbout this Structure
4fmn is a 3 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Gueneau E, Dherin C, Legrand P, Tellier-Lebegue C, Gilquin B, Bonnesoeur P, Londino F, Quemener C, Le Du MH, Marquez JA, Moutiez M, Gondry M, Boiteux S, Charbonnier JB. Structure of the MutLalpha C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site. Nat Struct Mol Biol. 2013 Apr;20(4):461-8. doi: 10.1038/nsmb.2511. Epub 2013 Feb , 24. PMID:23435383 doi:10.1038/nsmb.2511
- ↑ Habraken Y, Sung P, Prakash L, Prakash S. ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes. J Biol Chem. 1998 Apr 17;273(16):9837-41. PMID:9545323
- ↑ Wang TF, Kleckner N, Hunter N. Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13914-9. PMID:10570173
- ↑ Argueso JL, Kijas AW, Sarin S, Heck J, Waase M, Alani E. Systematic mutagenesis of the Saccharomyces cerevisiae MLH1 gene reveals distinct roles for Mlh1p in meiotic crossing over and in vegetative and meiotic mismatch repair. Mol Cell Biol. 2003 Feb;23(3):873-86. PMID:12529393
- ↑ Habraken Y, Sung P, Prakash L, Prakash S. ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes. J Biol Chem. 1998 Apr 17;273(16):9837-41. PMID:9545323
- ↑ Wang TF, Kleckner N, Hunter N. Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13914-9. PMID:10570173
- ↑ Erdeniz N, Dudley S, Gealy R, Jinks-Robertson S, Liskay RM. Novel PMS1 alleles preferentially affect the repair of primer strand loops during DNA replication. Mol Cell Biol. 2005 Nov;25(21):9221-31. PMID:16227575 doi:25/21/9221