Eshel D
Department of Biology, Brooklyn College, City University of New York 11210, USA.
Cell Motil Cytoskeleton. 1995;32(2):133-5. doi: 10.1002/cm.970320213.
The highly conserved lysine residue in the putative hydrolytic ATP-binding motif of the yeast cytoplasmic dynein heavy chain was replaced with leucine. The mutation was generated by a two-stage transformation method designed for genomic site-directed mutagenesis. Preliminary observations show that the effects of this alteration on the cellular roles of dynein are indistinguishable from those of a disruption mutation in which the entire motor domain is not expressed.
酵母细胞质动力蛋白重链假定的水解ATP结合基序中高度保守的赖氨酸残基被亮氨酸取代。该突变是通过一种为基因组定点诱变设计的两阶段转化方法产生的。初步观察表明，这种改变对动力蛋白细胞功能的影响与整个运动结构域不表达的缺失突变的影响无法区分。
