Glutamate promotes SSB protein-protein Interactions via intrinsically disordered regions.

ABSTRACT: E. coli single strand (ss) DNA binding protein (SSB) is an essential protein that binds to ssDNA intermediates formed during genome maintenance. SSB homotetramers bind ssDNA in several modes that differ in occluded site size and cooperativity. High "unlimited" cooperativity is associated with the 35 site size ((SSB)₃₅) mode at low [NaCl], whereas the 65 site size ((SSB)₆₅) mode formed at higher [NaCl] (> 200mM), where ssDNA wraps completely around the tetramer, displays "limited" cooperativity forming dimers of tetramers. It was previously thought that high cooperativity was associated only with the (SSB)₃₅ binding mode. However, we show here that highly cooperative binding also occurs in the (SSB)₆₅/(SSB)₅₆ binding modes at physiologi

SUBMITTER: Kozlov AG 

PROVIDER: S-EPMC5576569 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature