Abstract:
:Two cDNAs encoding casein kinase-1 have been isolated from a yeast cDNA library and termed CKI1 and CKI2. Each clone encodes a protein of approximately 62,000 Da containing a highly conserved protein kinase domain surrounded by variable amino- and carboxy-terminal domains. The proteins also contain two conserved carboxy-terminal cysteine residues that comprise a consensus sequence for prenylation. Consistent with this posttranslational modification, cell fractionation experiments demonstrate that intact CKI1 is found exclusively in yeast cell membranes. Gene disruption experiments reveal that, although neither of the two CKI genes is essential by itself, at least one CKI gene is required for yeast cell viability. Spores deficient in both CKI1 and CKI2 fail to grow and, therefore, either fail to germinate or arrest as small cells before bud emergence. These results suggest that casein kinase-1, which is distributed widely in nature, plays a pivotal role in eukaryotic cell regulation.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Wang PC,Vancura A,Mitcheson TG,Kuret Jdoi
10.1091/mbc.3.3.275keywords:
subject
Has Abstractpub_date
1992-03-01 00:00:00pages
275-86issue
3eissn
1059-1524issn
1939-4586journal_volume
3pub_type
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