Molecular mechanism of sequence-dependent stability of RecA filament
نویسندگان
چکیده
منابع مشابه
Molecular mechanism of sequence-dependent stability of RecA filament
RecA is a DNA-dependent ATPase and mediates homologous recombination by first forming a filament on a single-stranded (ss) DNA. RecA binds preferentially to TGG repeat sequence, which resembles the recombination hot spot Chi (5'-GCTGGTGG-3') and is the most frequent pattern (GTG) of the codon usage in Escherichia coli. Because of the highly dynamic nature of RecA filament formation, which consi...
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RecA protein (RecA) forms a nucleoprotein filament composed of a helical protein array that binds to singlestranded DNA (ssDNA), which in its active form is then able to initiate various reactions. A series of studies to date suggest the following roles of the N-terminal domain on filament formation by RecA. 1) The N-terminal domain of RecA is the functional region for protein-protein interacti...
متن کاملA RecA filament capping mechanism for RecX protein.
The RecX protein is a potent inhibitor of RecA protein activities. RecX functions by specifically blocking the extension of RecA filaments. In vitro, this leads to a net disassembly of RecA protein from circular single-stranded DNA. Based on multiple observations, we propose that RecX has a RecA filament capping activity. This activity has predictable effects on the formation and disassembly of...
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RecA K72R filament formation defects reveal an oligomeric RecA species involved in filament extension.
Using an ensemble approach, we demonstrate that an oligomeric RecA species is required for the extension phase of RecA filament formation. The RecA K72R mutant protein can bind but not hydrolyze ATP or dATP. When mixed with other RecA variants, RecA K72R causes a drop in the rate of ATP hydrolysis and has been used to study disassembly of hydrolysis-proficient RecA protein filaments. RecA K72R ...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2013
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gkt570