منابع مشابه
RecA
then most lines thereafter crossed out. Madame Auclair, the French violinist, had a gentler approach. Out of central casting, as they say: dark glasses, cigarette dangling, hoarse, accented voice. A friend went for a special violin lesson, and asked whether he might tape record this important event in his life. “Of course, my boy.” He played a bit and she said: “Very nice. There are some good t...
متن کاملRecA Protein
The RecA protein of Escherichia coli is the prototypic deoxyribonucleic acid (DNA) strand exchange protein. It assembles on single-stranded DNA to form a helical nucleoprotein filament that is the active species for all RecA protein-dependent functions. This protein– DNA complex is responsible for three mutually exclusive functions: DNA recombination, induction of the DNA-damage SOS response an...
متن کاملAffinity chromatography of RecA protein and RecA nucleoprotein complexes on RecA protein-agarose columns.
We have analyzed the nature of RecA protein-RecA protein interactions using an affinity column prepared by coupling RecA protein to an agarose support. When radiolabeled soluble proteins from Escherichia coli are applied to this column, only the labeled RecA protein from the extract was selectively retained and bound tightly to the affinity column. Efficient binding of purified 35S-labeled RecA...
متن کاملrecA protein-promoted ATP hydrolysis occurs throughout recA nucleoprotein filaments.
When recA protein binds cooperatively to single-stranded DNA to form filamentous nucleoprotein complexes, it becomes competent to hydrolyze ATP. No correlation exists between the ends of such complexes and the rate of ATP hydrolysis. ATP hydrolysis is not, therefore, restricted to the terminal subunits on cooperatively bound recA oligomers, but occurs throughout the complex. Similarly, during r...
متن کاملRecA protein dynamics in the interior of RecA nucleoprotein filaments.
We characterize aspects of the conformation and dynamic state of RecA filaments when bound to dsDNA that are specifically linked to the presence of the second of the two bound DNA strands. Filaments bound to dsDNA exhibit a facile exchange between free and bound RecA monomers or oligomers in the filament interior that is not seen on ssDNA. The RecA mutant K72R, which binds but does not hydrolyz...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Current Biology
سال: 2007
ISSN: 0960-9822
DOI: 10.1016/j.cub.2007.03.009