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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]
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 ]
DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. [ 3 ] [ 4 ] [ 5 ] Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA , because it exposes more functional groups that identify a base pair .
As with prokaryotes, two replisomes are required, one at each replication fork located at the terminus of the replication bubble. Because of significant differences in chromosome size, and the associated complexities of highly condensed chromosomes, various aspects of the DNA replication process in eukaryotes, including the terminal phases, are ...
Single-strand binding proteins stabilize the newly formed replication bubble and interact with the DnaG primase. DnaG recruits the replicative DNA polymerase III, and replication begins. In eukaryotes, MCM heterohexamer is phosphorylated by CDC7 and CDK, which displaces Cdc6 and recruits MCM10. MCM10 cooperates with MCM2-7 in the recruitment of ...
The major enzymatic functions carried out at the replication fork are well conserved from prokaryotes to eukaryotes, but the replication machinery in eukaryotic DNA replication is a much larger complex, coordinating many proteins at the site of replication, forming the replisome.
[1] The replication factor C, or RFC, is a five-subunit [2] protein complex that is required for DNA replication. The subunits of this heteropentamer are named Rfc1, Rfc2, Rfc3, Rfc4, and Rfc5 in Saccharomyces cerevisiae. RFC is used in eukaryotic replication as a clamp loader, similar to the γ Complex in Escherichia coli.