Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry.

ABSTRACT: Actin can exist in multiple conformations necessary for normal function. Actin isoforms, although highly conserved in sequence, exhibit different biochemical properties and cellular roles. We used amide proton hydrogen/deuterium (HD) exchange detected by mass spectrometry to analyze conformational differences between Saccharomyces cerevisiae and muscle actins in the G and F forms to gain insight into these differences. We also utilized HD exchange to study interdomain and allosteric communication in yeast-muscle hybrid actins to better understand the conformational dynamics of actin. Areas showing differences in HD exchange between G- and F-actins are areas of intermonomer contacts, consistent with the current filament models. Our results showed greater exchange for yeast G-actin compared

SUBMITTER: Stokasimov E 

PROVIDER: S-EPMC2757243 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature