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Site‐specific amino‐terminal mutants of yeast‐expressed β‐actin Characterization of the interaction with myosin and tropomyosin
Author(s) -
Aspenström Pontus,
Lindberg Uno,
Karlsson Roger
Publication year - 1992
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(92)80477-x
Subject(s) - tropomyosin , terminal (telecommunication) , yeast , myosin , mutant , actin , chemistry , biochemistry , amino terminal , microbiology and biotechnology , biology , peptide sequence , gene , computer science , telecommunications
Neutral or charge‐shifting, mutagenesis of β‐actin at positions 3 and 4 strongly influenced the actomyosin interaction under non‐rigor conditions. The polymerization behaviour and tropomyosin binding properties on the other hand remained unaffected.