CDKA and CDKB kinases from Chlamydomonas reinhardtii are able to complement cdc28 temperature-sensitive mutants of Saccharomyces cerevisiae
Jazyk angličtina Země Rakousko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- Chlamydomonas reinhardtii enzymologie MeSH
- cyklin-dependentní kinasy chemie metabolismus MeSH
- molekulární sekvence - údaje MeSH
- mutace genetika MeSH
- proteinkinasa CDC28, S cerevisiae metabolismus MeSH
- Saccharomyces cerevisiae cytologie enzymologie MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- teplota * MeSH
- testy genetické komplementace * MeSH
- transformace genetická MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- cyklin-dependentní kinasy MeSH
- proteinkinasa CDC28, S cerevisiae MeSH
Cyclin-dependent kinases (CDK) play a key role in coordinating cell division in all eukaryotes. We investigated the capability of cyclin-dependent kinases CDKA and CDKB from the green alga Chlamydomonas reinhardtii to complement a Saccharomyces cerevisiae cdc28 temperature-sensitive mutant. The full-length coding regions of algal CDKA and CDKB cDNA were amplified by RT-PCR and cloned into the yeast expression vector pYES-DEST52, yielding pYD52-CDKA and pYD52-CDKB. The S. cerevisiae cdc28-1N strain transformed with these constructs exhibited growth at 36 degrees C in inducing (galactose) medium, but not in repressing (glucose) medium. Microscopic observation showed that the complemented cells had the irregular cylindrical shape typical for G2 phase-arrested cells when grown on glucose at 36 degrees C, but appeared as normal budded cells when grown on galactose at 36 degrees C. Sequence analysis and complementation tests proved that both CDKA and CDKB are functional CDC28/cdc2 homologs in C. reinhardtii. The complementation of the mitotic phenotype of the S. cerevisiae cdc28-1N mutant suggests a mitotic role for both of the kinases.
Protoplasma. 2008;233(1-2):173 PubMed Umen, J G [added]
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