Hallmarks of homology recognition by RecA-like recombinases are exhibited by the unrelated Escherichia coli RecT protein
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چکیده
منابع مشابه
Polarity of heteroduplex formation promoted by Escherichia coli recA protein.
When recA protein pairs circular single strands with linear duplex DNA, the circular strand displaces its homolog from only one end of the duplex molecule and rapidly creates heteroduplex joints that are thousands of base pairs long [DasGupta, C., Shibata, T., Cunningham, R. P. & Radding, C. M. (1980) Cell 22, 437-446]. To examine this apparently polar reaction, we prepared chimeric duplex frag...
متن کاملEnhancement of Escherichia coli RecA protein enzymatic function by dATP.
The Escherichia coli recA protein has been shown to hydrolyze several nucleoside triphosphates in the presence of ssDNA. The substitution of dATP for rATP has significant effects on various recA protein biochemical properties. In the presence of dATP, recA protein can invade more secondary structure in native ssDNA than it can in the presence of rATP. The dATP-recA protein complex can compete m...
متن کاملInduction of the Bacillus subtilis SOS-like response by Escherichia coli RecA protein.
A plasmid that expresses the Escherichia coli RecA protein partially restored DNA repair and recombination capability and induction of the SOS-like (SOB) response in a recE4 mutant of Bacillus subtilis. In the presence of DNA-damaging agents, the E. coli RecA protein induced din operon expression, Weigle-reactivation activity, and synthesis of a B. subtilis recombination protein (Recbs) analogo...
متن کاملtif-1 mutation alters polynucleotide recognition by the recA protein of Escherichia coli.
The requirements for polynucleotide-dependent hydrolysis of ATP and for proteolytic cleavage of phage lambda repressor have been examined for both the wild-type (recA+ protein) and the tif-1 mutant form [tif(recA) protein] of the recA gene product. The recA+ and tif(recA) proteins catalyze both reactions in the presence of long single-stranded DNAs or certain deoxyhomopolymers. However, short o...
متن کاملInhibition of RecA protein by the Escherichia coli RecX protein: modulation by the RecA C terminus and filament functional state.
The RecX protein is a potent inhibitor of RecA activities. We identified several factors that affect RecX-RecA interaction. The interaction is enhanced by the RecA C terminus and by significant concentrations of free Mg(2+) ion. The interaction is also enhanced by an N-terminal His(6) tag on the RecX protein. We conclude that RecX protein interacts most effectively with a RecA functional state ...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2003
ISSN: 1460-2075
DOI: 10.1093/emboj/cdg027