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Functional dissection of the dynein motor domain

✍ Scribed by Eshel, Dan

Publisher: John Wiley and Sons
Year: 1995
Tongue: English
Weight: 260 KB
Volume: 32
Category: Article
ISSN: 0886-1544
DOI: 10.1002/cm.970320213

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✦ Synopsis

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.

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