| Literature DB >> 1879430 |
Abstract
Three N-terminal double mutants of beta-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.Entities:
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Year: 1991 PMID: 1879430 DOI: 10.1111/j.1432-1033.1991.tb21045.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956