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Exo1p

Protein FULL name:

5'-3' exonuclease and flap-endonuclease involved in recombination, double-strand break repair and DNA mismatch repair; member of the Rad2p nuclease family, with conserved N and I nuclease domains


Exo1p (Saccharomyces cerevisiae) is product of expression of EXO1 gene.


Exo1p is involved in:

MMR in Saccharomyces cerevisiae
     


Keywords:



FUNCTION: 5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.

COFACTOR: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding (By similarity).

ENZYME REGULATION: Inactivated by calcium and zinc ions.

SUBUNIT: Interacts with mismatch repair protein MSH2.

INTERACTION: P25847:MSH2; NbExp=3; IntAct=EBI-6738, EBI-11352; P43246:MSH2 (xeno); NbExp=1; IntAct=EBI-6738, EBI-355888;

SUBCELLULAR LOCATION: Nucleus (Potential).

MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.

SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.


NCBI GenPept GI number(s): 6324607
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P39875 P39875
PFAM: - P39875 (Link - using uniprot id)
InterPro: - P39875 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MGIQGLLPQLKPIQNPVSLRRYEGEVLAIDGYAWLHRAACSCAYELAMGK
PTDKYLQFFIKRFSLLKTFKVEPYLVFDGDAIPVKKSTESKRRDKRKENK
AIAERLWACGEKKNAMDYFQKCVDITPEMAKCIICYCKLNGIRYIVAPFE
ADSQMVYLEQKNIVQGIISEDSDLLVFGCRRLITKLNDYGECLEICRDNF
IKLPKKFPLGSLTNEEIITMVCLSGCDYTNGIPKVGLITAMKLVRRFNTI
ERIILSIQREGKLMIPDTYINEYEAAVLAFQFQRVFCPIRKKIVSLNEIP
LYLKDTESKRKRLYACIGFVIHRETQKKQIVHFDDDIDHHLHLKIAQGDL
NPYDFHQPLANREHKLQLASKSNIEFGKTNTTNSEAKVKPIESFFQKMTK
LDHNPKVANNIHSLRQAEDKLTMAIKRRKLSNANVVQETLKDTRSKFFNK
PSMTVVENFKEKGDSIQDFKEDTNSQSLEEPVSESQLSTQIPSSFITTNL
EDDDNLSEEVSEVVSDIEEDRKNSEGKTIGNEIYNTDDDGDGDTSEDYSE
TAESRVPTSSTTSFPGSSQRSISGCTKVLQKFRYSSSFSGVNANRQPLFP
RHVNQKSRGMVYVNQNRDDDCDDNDGKNQITQRPSLRKSLIGARSQRIVI
DMKSVDERKSFNSSPILHEESKKRDIETTKSSQARPAVRSISLLSQFVYK
GK

Exo1p (Saccharomyces cerevisiae) is able to recognize following damages:
References:

Title Authors Journal
Molecular cloning of a gene, DHS1, which complements a drug-hypersensitive mutation of the yeast Saccharomyces cerevisiae. Lee YS, Shimizu J, Yoda K, Yamasaki M Biosci Biotechnol Biochem Jan. 1, 1994
The nucleotide sequence of Saccharomyces cerevisiae chromosome XV. Dujon B, Albermann K, Aldea M, Alexandraki D, Ansorge W, Arino J, Benes V, Bohn C, Bolotin-Fukuhara M, Bordonne R, Boyer J, Camasses A, Casamayor A, Casas C, Cheret G, Cziepluch C, Daignan-Fornier B, Dang DV, de Haan M, Delius H, Durand P, Fairhead C, Feldmann H, Gaillon L, Kleine K, et al. Nature May 1, 1997
Exonuclease I of Saccharomyces cerevisiae functions in mitotic recombination in vivo and in vitro. Fiorentini P, Huang KN, Tishkoff DX, Kolodner RD, Symington LS Mol Cell Biol May 1, 1997
Identification and characterization of Saccharomyces cerevisiae EXO1, a gene encoding an exonuclease that interacts with MSH2. Tishkoff DX, Boerger AL, Bertrand P, Filosi N, Gaida GM, Kane MF, Kolodner RD Proc Natl Acad Sci U S A July 8, 1997
Decreased meiotic intergenic recombination and increased meiosis I nondisjunction in exo1 mutants of Saccharomyces cerevisiae. Kirkpatrick DT, Ferguson JR, Petes TD, Symington LS Genetics Dec. 1, 2000
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
Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective cells. Cotta-Ramusino C, Fachinetti D, Lucca C, Doksani Y, Lopes M, Sogo J, Foiani M Mol Cell Feb. 7, 2005
Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Smolka MB, Albuquerque CP, Chen SH, Zhou H Proc Natl Acad Sci U S A June 19, 2007
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics July 1, 2008


Last modification of this entry: Oct. 12, 2010.

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