Site-specific amino-terminal mutants of yeast-expressed beta-actin. Characterization of the interaction with myosin and tropomyosin.
Neutral or charge-shifting mutagenesis of beta-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.
Aspenström
P
P
Dept. Developmental Biology, Uppsala University, Sweden.
Lindberg
U
U
Karlsson
R
R
D000199:Actins / Q000235:genetics* / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005800:Genes, Fungal; D016297:Mutagenesis, Site-Directed; D009218:Myosins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014335:Tropomyosin / Q000378:metabolism*
D000199:Actins; D014335:Tropomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins