| Autor: |
Winkler AA; Institute for Molecular Plant Sciences, Leiden, The Netherlands., Bobok A, Zonneveld BJ, Steensma HY, Hooykaas PJ |
| Jazyk: |
angličtina |
| Zdroj: |
Yeast (Chichester, England) [Yeast] 1998 Jan 15; Vol. 14 (1), pp. 37-48. |
| DOI: |
10.1002/(SICI)1097-0061(19980115)14:1<37::AID-YEA198>3.0.CO;2-2 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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