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Conformational changes in subdomain‐2 of G‐actin upon polymerization into F‐actin and upon binding myosin subfragment‐1
Author(s) -
Fievez Stéphane,
Carlier Marie-France
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81212-i
Subject(s) - myosin , actin , polymerization , biophysics , chemistry , actin binding protein , actin remodeling , conformational change , biochemistry , polymer , biology , cytoskeleton , actin cytoskeleton , organic chemistry , cell
The susceptibility of subdomain‐2 of actin to different proteases has been examined, for G‐actin, F‐actin, G‐actin‐S 1 (A 2 ) and F‐actin‐S 1 (A 2 ) complexes on a comparative basis. The sites of subtilisin, α‐chymotrypsin and trypsin attack, exposed on G‐actin, are protected in F‐actin, F‐actin‐S 1 (A 2 ) as well as in the G‐actin‐S 1 (A 2 ) complex. In contrast, a new cleavage site (Arg 39 ‐His 40 ) for ArgC protease, which is protected in G‐actin, is exposed in G‐actin‐S 1 (A 2 ) as well as in F‐actin and F‐actin‐S 1 (A 2 ). These results are consistent with the previously proposed structural analogy between the ternary (G‐actin) 2 S 1 and the F‐actin‐S 1 complexes, and provide information on the mechanism of S 1 ‐induced polymerization of G‐actin.