Open AccessInterference with myosin subfragment‐1 binding by site‐directed mutagenesis of actin
Author(s) -
ASPENSTRÖM Pontus,
KARLSSON Roger
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb21045.x
Subject(s) - myosin , saccharomyces cerevisiae , actin , yeast , actin binding protein , mutagenesis , site directed mutagenesis , biochemistry , binding site , mutant , actina , chemistry , microbiology and biotechnology , biophysics , biology , actin cytoskeleton , cytoskeleton , gene , cell
Three N‐terminal double mutants of β‐actin expressed in the yeast Saccharomyces cerevisiae have been characterized with respect to DNase‐I interaction, N‐terminal post‐translational modification, polymerizability and myosin subfragment‐1 binding. The results strongly support earlier suggestions that the acidic residues at the N‐terminus of actin are part of the myosin‐binding site, while they seem to be of no importance for the other aspects of actin biochemistry tested. The suitability of this expression system for production of recombinant actin in general is discussed.