About: The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity

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About: The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 1999

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1999 (uk) im Januar 1999 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1999 (ast) artikull shkencor i botuar më 01 janar 1999 (sq) scientific article published on 01 January 1999 (en)
publication date	wds:Q77765360-89099820-033D-4058-B7A3-CD3711FCDAE5
publication date	1999-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q77765360-B2502DC2-D327-406C-9836-244CD8AD3EC8
language of work or name	English
cites work	wds:Q77765360-186BEFF6-DDBD-4902-8F33-1CB66922DAE6 wds:Q77765360-20F3DD25-8535-467D-951D-5870A71EE437 wds:Q77765360-411A42D6-115D-4E82-B39E-238E46C9EE6E wds:Q77765360-469C7D89-53CE-4BD0-A469-38D30577070E wds:Q77765360-4CAD4864-F24D-4D4B-A279-0734703805D6 wds:Q77765360-52220E95-21EB-4B9B-A93B-153A7F43758B wds:Q77765360-5A36B230-6CA2-4C68-BC74-61934A4E03DA wds:Q77765360-63CF9E2A-269D-492F-9D05-878B81ADF3D5 wds:Q77765360-8280572C-6395-4CC6-8A4C-28BF9BC065A9 wds:Q77765360-8AC59CB5-BA17-4363-A34A-5FBE1FC3A045 wds:Q77765360-95E2CF84-CC7B-4C32-8BDA-DEAE2BDD0D10 wds:Q77765360-9A160E93-FB3F-44E2-A322-D67C863610F5 wds:Q77765360-A1956378-5FF2-4CA0-9E85-2B83BA98F04A wds:Q77765360-AE3C8AC6-7A8F-451A-A9B8-0B995920A87C wds:Q77765360-D18534D7-67D7-4F1A-A7F5-4CAEEFD78967 wds:Q77765360-D266F932-3237-4CB0-9D38-61147D45047D
cites work	Role of MutS ATPase activity in MutS,L-dependent block of in vitro strand transfer Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis Cloning and nucleotide sequence of DNA mismatch repair gene PMS1 from Saccharomyces cerevisiae: homology of PMS1 to procaryotic MutL and HexB. Dual requirement in yeast DNA mismatch repair for MLH1 and PMS1, two homologs of the bacterial mutL gene MutS mediates heteroduplex loop formation by a translocation mechanism MutS and MutL activate DNA helicase II in a mismatch-dependent manner Mismatch repair in replication fidelity, genetic recombination, and cancer biology Mismatch-, MutS-, MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex Molecular matchmakers Positionally cloned human disease genes: patterns of evolutionary conservation and functional motifs Mechanisms and biological effects of mismatch repair Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs DNA mismatch correction in a defined system Methyl-directed repair of DNA base-pair mismatches in vitro Double helicase II (uvrD)-helicase IV (helD) deletion mutants are defective in the recombination pathways of Escherichia coli Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD.
author name string	wds:Q77765360-9D060A7D-180E-44E1-8CD2-8315F7BB75D0
author name string	S W Matson
rdfs:label	The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (en) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (nl) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (sq)
skos:prefLabel	The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (en) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (nl) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (sq)
name	The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (en) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (nl) The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (sq)
author	wds:Q77765360-DCB843B3-1A53-4B40-84C5-5CC12EF1D1AA
author	Mark C Hall
title	wds:Q77765360-EA34C693-660C-44C7-A5C7-640DE2081AA5
title	The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity (en)
page(s)	wds:Q77765360-EAB59CAF-2535-428C-B2BD-8F90172B9C91
page(s)	1306-1312
instance of	wds:Q77765360-41EEB98C-FFCA-4263-B72E-48FD0B01EE52
instance of	scholarly article
main subject	wds:Q77765360-BFA091BB-FE14-402D-B23E-E49522B3C15F
main subject	Escherichia coli
PubMed ID	wds:Q77765360-461299DE-57EF-4996-85ED-30A8A0A6FB19
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9880500
PubMed ID	9880500
published in	wds:Q77765360-0F7438CA-1140-4CDE-9CE7-247F106F9EA2
published in	Journal of Biological Chemistry
issue	wds:Q77765360-26D441DB-B314-4F00-A8EC-9B2DE220916A
volume	wds:Q77765360-20AD7EBA-E9C2-474D-A55F-D54FCADC03F9
issue	3
volume	274
number of pages	wds:Q77765360-FBB35F2A-4E76-417C-B977-89E76A6EF318
number of pages	7 (xsd:decimal)
DOI	wds:Q77765360-A515FB02-6F3D-4AEC-862C-D126EE9576D2
DOI	http://dx.doi.org/10.1074/JBC.274.3.1306
DOI	10.1074/JBC.274.3.1306
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q77765360
is cites work of	Spontaneous conversion between mutL and 6 bpDeltamutL in Salmonella typhimurium LT7: association with genome diversification and possible roles in bacterial adaptation. The role of the human DNA mismatch repair gene hMSH2 in DNA repair, cell cycle control and apoptosis: implications for pathogenesis, progression and therapy of cancer Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair Extensive microsatellite variation in rice induced by introgression from wild rice (Zizania latifolia Griseb.). The interaction of DNA mismatch repair proteins with human exonuclease I Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6 hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA. Analysis of the human MutLalpha.MutSalpha complex Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha The alternating ATPase domains of MutS control DNA mismatch repair Structure and function of mismatch repair proteins Identifying an interaction site between MutH and the C-terminal domain of MutL by crosslinking, affinity purification, chemical coding and mass spectrometry Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair Evolution of the methyl directed mismatch repair system in Escherichia coli. Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA. Interaction of Escherichia coli MutS and MutL at a DNA mismatch Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair

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