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The lysine‐rich C‐terminal repeats of the centromere‐binding factor 5 (Cbf5) of Kluyveromyces lactis are not essential for function
Author(s) -
Winkler A. A.,
Bobok A.,
Zonneveld B. J. M.,
Steensma H. Y.,
Hooykaas P. J. J.
Publication year - 1998
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/(sici)1097-0061(19980115)14:1<37::aid-yea198>3.0.co;2-2
Subject(s) - biology , kluyveromyces lactis , plasmid , microbiology and biotechnology , saccharomyces cerevisiae , complementation , centromere , gene , genetics , biochemistry , chromosome , phenotype
The gene coding for the centromere‐binding factor 5 ( CBF5 ) of Kluyveromyces lactis has been isolated by hybridization of a Saccharomyces cerevisiae CBF5 DNA probe to a K. lactis library. The amino acid sequence of KlCbf5 is highly homologous, 88% identity, to ScCbf5, but also to the rat protein Nap57 (64% identity). The main difference between both yeast proteins and the rat protein is the presence of a lysine‐rich domain with KKE/D repeats in the C‐terminal part of the protein. These repeats are thought to be involved in binding of the protein to microtubules. Deletion of the KKE/D domain in KlCbf5 however, has no discernible effect on growth on rich medium, sensitivity to the microtubule‐destabilizing drug benomyl or segregation of a reporter plasmid. On the other hand, insertion of two leucine residues adjacent to the KKE domain increases the loss rate of a reporter plasmid. In both yeasts complementation of a lethal CBF5 disruption with the heterologous gene results in a slight increase in benomyl sensitivity. A possible role of CBF5 in chromosome segregation will be discussed. © 1998 John Wiley & Sons, Ltd.