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Single-stranded DNA is produced during all aspects of DNA metabolism: replication, recombination, and repair. As well as stabilizing this single-stranded DNA, SSB proteins bind to and modulate the function of numerous proteins involved in all of these processes. Active E. coli SSB is composed of four identical 19 kDa subunits. Binding of single ...
In ICP8, the herpes simplex virus (HSV-1) single-strand DNA-binding protein (ssDNA-binding protein (SSB)), the head consists of the eight alpha helices.The front side of the neck region consists of a five-stranded beta-sheet and two alpha helices, whereas the back side is a three-stranded beta-sheet The shoulder part of the N-terminal domain contains an alpha-helical and beta-sheet region. [1]
To counteract this instability, single-strand binding proteins (SSB in prokaryotes and Replication protein A in eukaryotes) bind to the exposed bases to prevent improper ligation. If you consider each strand as a "dynamic, stretchy string", the structural potential for improper ligation should be obvious.
Replication protein A (RPA) is the major protein that binds to single-stranded DNA (ssDNA) in eukaryotic cells. [ 1 ] [ 2 ] In vitro , RPA shows a much higher affinity for ssDNA than RNA or double-stranded DNA. [ 3 ]
The SSB protein interacts with DNA helicases PriA and RecG to recover stalled DNA replication forks. These enzymes must bind to the SSB-helicase to be loaded onto stalled forks. Thermal sliding and DNA duplex binding are possibly supported by the wedge domain of RecG's association with the SSB linker.
A distinct group of DNA-binding proteins are the DNA-binding proteins that specifically bind single-stranded DNA. In humans, replication protein A is the best-understood member of this family and is used in processes where the double helix is separated, including DNA replication, recombination and DNA repair. [18]
Replication restart is a multi-step process in E. coli that requires the sequential action of several proteins. When the progress of the replication fork is impeded the proteins single-stranded binding protein SSB and RecG helicase along with the RuvABC complex are required for rescue. [2]
The small, excised, damage-containing DNA (sedDNA) oligonucleotides are initially released from the duplex in complex with TFIIH but then dissociate in an ATP-dependent manner and become bound to replication protein A (RPA). Inhibition of gap filling DNA synthesis and ligation results in an accumulation of RPA-bound sedDNAs in the cell.