title: Functional dissection of the dynein motor domain.
abstract: 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.
authors.affiliation: Department of Biology, Brooklyn College, City University of New York 11210, USA.
authors.forename: D
authors.initials: D
authors.lastname: Eshel
mesh_terms: D000595:Amino Acid Sequence; D015825:Chromosomes, Fungal; D004398:Dyneins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005796:Genes; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D008941:Spindle Apparatus; D013329:Structure-Activity Relationship
chemical_list: D005656:Fungal Proteins; D004398:Dyneins