The KlHEM1 gene from Kluyveromyces lactis encodes a functional 5-aminolevulinate synthase ( ALA synthase), as confirmed by complementation of a hem1 mutant Saccharomyces cerevisiae strain, homology search, and detection of a 2β’3 kb transcript. The gene is highly homologous to the ScHEM1 gene, and th
Identification and characterization of theKlCMD1 gene encodingKluyveromyces lactis calmodulin
β Scribed by Rayner, Timothy F.; Stark, Michael J. R.
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 166 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0749-503X
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β¦ Synopsis
The KlCMD1 gene was isolated from a Kluyveromyces lactis genomic library as a suppressor of the Saccharomyces cerevisiae temperature-sensitive mutant spc110-124, an allele previously shown to be suppressed by elevated copy number of the S. cerevisiae calmodulin gene CMD1. The KlCMD1 gene encodes a polypeptide which is 95% identical to S. cerevisiae calmodulin and 55% identical to calmodulin from Schizosaccharomyces pombe.
Complementation of a S. cerevisiae cmd1 deletion mutant by KlCMD1 demonstrates that this gene encodes a functional calmodulin homologue. Multiple sequence alignment of calmodulins from yeast and multicellular eukaryotes shows that the K. lactis and S. cerevisiae calmodulins are considerably more closely related to each other than to other calmodulins, most of which have four functional Ca 2+ -binding EF hand domains. Thus like its S. cerevisiae counterpart Cmd1p, the KlCMD1 product is predicted to form only three Ca 2+ -binding motifs.
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