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Msh3p

Protein FULL name:

Mismatch repair protein, forms dimers with Msh2p that mediate repair of insertion or deletion mutations and removal of nonhomologous DNA ends, contains a PCNA (Pol30p) binding motif required for genome stability


Msh3p (Saccharomyces cerevisiae) is product of expression of MSH3 gene.


Msh3p is involved in:

MMR in Saccharomyces cerevisiae
     


Keywords:



FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate-specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with either the MutL alpha or MutL beta heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and NHTR.

SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta (MLH1-MLH3). MutS beta interacts with proliferating cell nuclear antigen (PCNA/POL30). Interacts with SAW1.

INTERACTION: P50277:BIO3; NbExp=1; IntAct=EBI-11362, EBI-3632; P02293:HTB1; NbExp=1; IntAct=EBI-11362, EBI-8088; P47017:LSM1; NbExp=1; IntAct=EBI-11362, EBI-174; P32266:MGM1; NbExp=1; IntAct=EBI-11362, EBI-10865;

SUBCELLULAR LOCATION: Nucleus.

DOMAIN: The PIP box serves as a PCNA(POL30)-recognition and -binding motif.

MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.

SIMILARITY: Belongs to the DNA mismatch repair mutS family. MSH3 subfamily.

SEQUENCE CAUTION: Sequence=AAA34803.1; Type=Erroneous initiation; Sequence=CAA42247.1; Type=Erroneous initiation; Sequence=CAA46116.1; Type=Erroneous initiation;


NCBI GenPept GI number(s): 157285763
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P25336 P25336
PFAM: - P25336 (Link - using uniprot id)
InterPro: - P25336 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSS
VASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKR
RSDENVEAEDDEEEGEEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRDKV
LVIRVGYKYKCFAEDAVTVSRILHIKLVPGKLTIDESNPQDCNHRQFAYC
SFPDVRLNVHLERLVHHNLKVAVVEQAETSAIKKHDPGASKSSVFERKIS
NVFTKATFGVNSTFVLRGKRILGDTNSIWALSRDVHQGKVAKYSLISVNL
NNGEVVYDEFEEPNLADEKLQIRIKYLQPIEVLVNTDDLPLHVAKFFKDI
SCPLIHKQEYDLEDHVVQAIKVMNEKIQLSPSLIRLVSKLYSHMVEYNNE
QVMLIPSIYSPFASKIHMLLDPNSLQSLDIFTHDGGKGSLFWLLDHTRTS
FGLRMLREWILKPLVDVHQIEERLDAIECITSEINNSIFFESLNQMLNHT
PDLLRTLNRIMYGTTSRKEVYFYLKQITSFVDHFKMHQSYLSEHFKSSDG
RIGKQSPLLFRLFSELNELLSTTQLPHFLTMINVSAVMEKNSDKQVMDFF
NLNNYDCSEGIIKIQRESESVRSQLKEELAEIRKYLKRPYLNFRDEVDYL
IEVKNSQIKDLPDDWIKVNNTKMVSRFTTPRTQKLTQKLEYYKDLLIRES
ELQYKEFLNKITAEYTELRKITLNLAQYDCILSLAATSCNVNYVRPTFVN
GQQAIIAKNARNPIIESLDVHYVPNDIMMSPENGKINIITGPNMGGKSSY
IRQVALLTIMAQIGSFVPAEEIRLSIFENVLTRIGAHDDIINGDSTFKVE
MLDILHILKNCNKRSLLLLDEVGRGTGTHDGIAISYALIKYFSELSDCPL
ILFTTHFPMLGEIKSPLIRNYHMDYVEEQKTGEDWMSVIFLYKLKKGLTY
NSYGMNVAKLARLDKDIINRAFSISEELRKESINEDALKLFSSLKRILKS
DNITATDKLAKLLSLDIH

Msh3p (Saccharomyces cerevisiae) is able to recognize following damages:
Msh3p (Saccharomyces cerevisiae) belongs to following protein families:
References:

Title Authors Journal
The sequence of a 6.3 kb segment of yeast chromosome III reveals an open reading frame coding for a putative mismatch binding protein. Valle G, Bergantino E, Lanfranchi G, Carignani G Yeast Dec. 1, 1991
The complete DNA sequence of yeast chromosome III. Oliver SG, van der Aart QJ, Agostoni-Carbone ML, Aigle M, Alberghina L, Alexandraki D, Antoine G, Anwar R, Ballesta JP, Benit P, et al. Nature May 7, 1992
The yeast gene MSH3 defines a new class of eukaryotic MutS homologues. New L, Liu K, Crouse GF Mol Gen Genet May 1, 1993
Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair. Marsischky GT, Filosi N, Kane MF, Kolodner R Genes Dev Jan. 15, 1996
Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3. Habraken Y, Sung P, Prakash L, Prakash S Curr Biol Sept. 1, 1996
Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair. Johnson RE, Kovvali GK, Guzder SN, Amin NS, Holm C, Habraken Y, Sung P, Prakash L, Prakash S J Biol Chem Nov. 8, 1996
Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes. Sia EA, Kokoska RJ, Dominska M, Greenwell P, Petes TD Mol Cell Biol May 1, 1997
Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination. Sugawara N, Paques F, Colaiacovo M, Haber JE Proc Natl Acad Sci U S A Aug. 19, 1997
Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex. Habraken Y, Sung P, Prakash L, Prakash S Curr Biol Oct. 1, 1997
The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations. Flores-Rozas H, Kolodner RD Proc Natl Acad Sci U S A Oct. 13, 1998
Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination. Studamire B, Price G, Sugawara N, Haber JE, Alani E Mol Cell Biol Nov. 1, 1999
Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes. Clark AB, Valle F, Drotschmann K, Gary RK, Kunkel TA J Biol Chem Nov. 24, 2000
Sequencing and comparison of yeast species to identify genes and regulatory elements. Kellis M, Patterson N, Endrizzi M, Birren B, Lander ES Nature May 15, 2003
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature Oct. 16, 2003
Global analysis of protein localization in budding yeast. Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, O'Shea EK Nature Oct. 16, 2003
Analysis of the proteins involved in the in vivo repair of base-base mismatches and four-base loops formed during meiotic recombination in the yeast Saccharomyces cerevisiae. Stone JE, Petes TD Genetics July 1, 2006
Mismatch repair factor MSH2-MSH3 binds and alters the conformation of branched DNA structures predicted to form during genetic recombination. Surtees JA, Alani E J Mol Biol July 14, 2006
Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition. Lee SD, Surtees JA, Alani E J Mol Biol Jan. 9, 2007
Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins. Shell SS, Putnam CD, Kolodner RD Proc Natl Acad Sci U S A June 26, 2007
Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs. Harrington JM, Kolodner RD Mol Cell Biol Sept. 1, 2007
Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates. Li F, Dong J, Pan X, Oum JH, Boeke JD, Lee SE Mol Cell May 9, 2008


Last modification of this entry: Oct. 13, 2010.

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