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Nucleic Acids Research, 1987, Vol. 15, No. 20 8439-8450
© 1987


Articles

Metal-binding, nucleic acid-binding finger sequences in the CDC16 gene of Saccharomyces cerevisiae

Tateo Icho and Reed B. Wickner

Section on Genetics of Simple Eukaryotes, Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health Building 8, Room 209, Bethesda, MD 20892, USA

Received September 2, 1987. Accepted September 22, 1987.

The CDC16 gene is involved in the process of chromosome segregation in mitosis and a cdc16 mutant accumulates the predominant microtubule-associated protein at the nonpermissive temperature. We find that the CDC16 gene open reading frame (ORF) is capable of encoding a protein whose calculated molecular weight and pI are 94, 967 and 6.60, respectively. This hypothetical protein contains 16 cysteine residues; five are clustered at the N-terminal, 4 are placed about 3 residues apart in the middle of the pep tide, and 3- are located close to the C-terminal. Each of these could form a metal-binding, nucleic acid-binding domain, suggesting this protein acts either as a repres-sor of the microtubule-associated protein gene or as a component necessary for spindle elongation, possibly interacting with the DNA. The start of the CDC16 ORF is only 95 bp downstream from the end of the MAK11 ORF. In this region there are two TATA boxes in tandem, but there is no room for a DAS or other regulatory sequences. An ATG is present 5 bp upstream of the start of the large ORF. Its frame terminates after only two amino acids.


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