Regulation of Nearest-Neighbor Cooperative Binding of E. coli SSB Protein to DNA.

ABSTRACT: Escherichia coli single-strand (ss) DNA-binding protein (SSB) is an essential protein that binds ssDNA intermediates formed during genome maintenance. SSB homotetramers bind ssDNA in several modes differing in occluded site size and cooperativity. The 35-site-size ((SSB)₃₅) mode favored at low [NaCl] and high SSB/DNA ratios displays high "unlimited" nearest-neighbor cooperativity (ω₃₅), forming long protein clusters, whereas the 65-site-size ((SSB)₆₅) mode in which ssDNA wraps completely around the tetramer is favored at higher [NaCl] (>200 mM) and displays "limited" cooperativity (ω₆₅), forming only dimers of tetramers. In addition, a non-nearest-neighbor high cooperativity can also occur in the (SSB)₆₅ mode on long ssDNA even at phys

SUBMITTER: Kozlov AG 

PROVIDER: S-EPMC6895745 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature