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Titolo:
The efficiency of strand invasion by Escherichia coli RecA is dependent upon the length and polarity of ssDNA tails
Autore:
McIlwraith, MJ; West, SC;
Indirizzi:
Imperial Canc Res Fund, Clare Hall Labs, S Mimms EN6 3LD, Herts, England Imperial Canc Res Fund S Mimms Herts England EN6 3LD 3LD, Herts, England
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 305, anno: 2001,
pagine: 23 - 31
SICI:
0022-2836(20010105)305:1<23:TEOSIB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
JOINT MOLECULE FORMATION; DNA-BINDING PROTEINS; HUMAN RAD51 PROTEIN; RECBCD ENZYME; HETERODUPLEX FORMATION; BRANCH MIGRATION; RECOMBINATION HOTSPOT; PLECTONEMIC JOINTS; RUVABC PROTEINS; ATP HYDROLYSIS;
Keywords:
recombination; repair; D-loops; strand exchange; SOS response;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: West, SC Imperial Canc Res Fund, Clare Hall Labs, S Mimms EN6 3LD, Herts, England Imperial Canc Res Fund S Mimms Herts England EN6 3LD ts, England
Citazione:
M.J. McIlwraith e S.C. West, "The efficiency of strand invasion by Escherichia coli RecA is dependent upon the length and polarity of ssDNA tails", J MOL BIOL, 305(1), 2001, pp. 23-31

Abstract

RecA protein is essential for homologous recombination and the repair of DNA double-strand breaks in Escherichia coli. The protein binds DNA to form nucleoprotein filaments that promote joint molecule formation and strand exchange in vitro. RecA polymerises on ssDNA in the 5'-3' direction and catalyses strand exchange and branch migration with a 5'-3' polarity. It has been reported previously, using D-loop assays, in which ssDNA (containing a heterologous block at one end) invades supercoiled duplex DNA that 3'-homologous ends are reactive, whereas 5'-ends are inactive. This polarity bias wasthought to be due to the polarity of RecA filament formation, which results in the 3'-ends being coated in RecA, whereas 5'-ends remain naked. Using a range of duplex substrates containing ssDNA tails of various lengths and polarities, we now demonstrate that when no heterologous block is imposed, 5'-ends are just as reactive as 3'-ends. Moreover, using short-tailed substrates, we find that 5'-ends form more stable D-loops than 3'-ends. This bias may be a consequence of the instability of short 3'-joints. With more physiological substrates containing long ssDNA tails, we find that RecA shows no intrinsic preference for 5' or 3'-ends and that both form D-loop complexes with high efficiency. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 18:26:22