Electronic Resource
New York, NY
:
Wiley-Blackwell
Cell Motility and the Cytoskeleton
32 (1995), S. 133-135
ISSN:
0886-1544
Keywords:
cytoplasmic dynein
;
motor domain
;
mutational analysis
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
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. © 1995 Wiley-Liss, Inc.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970320213
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