RecA protein forms filaments on both single- and dou-ble-stranded DNA. Several studies confirm that filament extension occurs in the 5 to 3 direction on single-stranded DNA. These filaments also disassemble in an end-dependent fashion, and several indirect observa-tions suggest that the disassembly occurs on the end opposite to that at which assembly occurs. By labeling the 5 end of single-stranded DNA with a segment of duplex DNA, we demonstrate unambiguously that RecA filaments disassemble uniquely in the 5 to 3 direction. The active form of the bacterial RecA protein is a filament formed on DNA. RecA has no known activities when it is not part of such a filamentous complex. Further, the action of several other bacterial proteins app...
<p>At the core of homologous DNA repair, RecA catalyzes the strand exchange reaction. This process i...
AbstractThe crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it ...
The RecA protein forms nucleoprotein filaments on DNA, and individual monomers within the filaments ...
characterize aspects of the conformation and dynamic state of RecA University of filaments when boun...
RecA protein primarily associates with and disso-ciates from opposite ends of nucleoprotein filament...
<div><p>(A) RecA filaments can nucleate on dsDNA so as to have two different orientations. The initi...
To further characterize the role of RecA protein-DNA filaments in general recombination and DNA repa...
To further characterize the role of RecA protein-DNA filaments in general recombination and DNA repa...
RecA, the key protein in homologous recombination, performs its actions as a helical filament on sin...
RecA, the key protein in homologous recombina-tion, performs its actions as a helical filament on si...
In the presence of ATP, recA protein forms a presynaptic complex with single-stranded DNA that is an...
In the presence of ATP, recA protein forms a presynaptic complex with single-stranded DNA that is an...
textabstractRecA, the key protein in homologous recombination, performs its actions as a helical fil...
RecA, the key protein in homologous recombination, performs its actions as a helical filament on sin...
When E. coli single-stranded DNA binding protein (SSB) coats single-stranded DNA (ssDNA) in the pres...
<p>At the core of homologous DNA repair, RecA catalyzes the strand exchange reaction. This process i...
AbstractThe crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it ...
The RecA protein forms nucleoprotein filaments on DNA, and individual monomers within the filaments ...
characterize aspects of the conformation and dynamic state of RecA University of filaments when boun...
RecA protein primarily associates with and disso-ciates from opposite ends of nucleoprotein filament...
<div><p>(A) RecA filaments can nucleate on dsDNA so as to have two different orientations. The initi...
To further characterize the role of RecA protein-DNA filaments in general recombination and DNA repa...
To further characterize the role of RecA protein-DNA filaments in general recombination and DNA repa...
RecA, the key protein in homologous recombination, performs its actions as a helical filament on sin...
RecA, the key protein in homologous recombina-tion, performs its actions as a helical filament on si...
In the presence of ATP, recA protein forms a presynaptic complex with single-stranded DNA that is an...
In the presence of ATP, recA protein forms a presynaptic complex with single-stranded DNA that is an...
textabstractRecA, the key protein in homologous recombination, performs its actions as a helical fil...
RecA, the key protein in homologous recombination, performs its actions as a helical filament on sin...
When E. coli single-stranded DNA binding protein (SSB) coats single-stranded DNA (ssDNA) in the pres...
<p>At the core of homologous DNA repair, RecA catalyzes the strand exchange reaction. This process i...
AbstractThe crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it ...
The RecA protein forms nucleoprotein filaments on DNA, and individual monomers within the filaments ...