A split zinc-finger protein is required for normal yeast growth.
Gene. 1991; 107: 101-10
We have identified a gene that, when present in multiple copies, partially inhibits nuclear protein localization in Saccharomyces cerevisiae. This gene encodes a protein that is a unique member of the Cys2His2 zinc-finger family of DNA-binding proteins. It is designated SFP1 for split finger protein because its two zinc-finger domains are separated from one another by 40 amino acids (aa) as opposed to the usual spacing of 7 or 8 aa for Cys2His2 proteins. Disruption of the SFP1 gene results in slow cell growth, with cells having multiple, nucleated buds.
Potential DNA-binding domains in the RAD18 gene product of Saccharomyces cerevisiae.
Gene. 1988; 74: 543-7
The RAD18 gene of Saccharomyces cerevisiae is involved in the error-prone DNA repair. Its nucleotide sequence, as reported here, predicts an open reading frame of 1461 nt which corresponds to a protein of 487 amino acids, with an Mr of 55,237. This protein has three putative zinc fingers, two acidic regions and a nucleotide-binding domain, suggesting that it is a nucleic acid-binding protein with a possible regulatory role.