Nature. 1992 May 28;357(6376):301-6.

Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae.

Source

Department of Molecular and Cell Biology, University of California, Berkeley 94720.

Abstract

An unusual protein splicing reaction joins the N-terminal segment (A) and the C-terminal segment (C) of the 119K primary translation product (ABC) of the yeast VMA1 gene to yield a 69K vacuolar H(+)-ATPase subunit (AC) and an internal 50K polypeptide (B). This 50K protein is a site-specific DNA endonuclease that shares 34% identity with the homothallic switching endonuclease. The site cleaved by the VMA1-derived endonuclease exists in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame. Cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking the endonuclease coding sequence into one that contains it.

PMID:: 1534148; [PubMed - indexed for MEDLINE]

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Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. [J Biol Chem. 1990]
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Structures reported by this article

Pi-Scei, A Homing Endonuclease With Protein Splicing Activity

PDB: 1VDE

Source: Saccharomyces cerevisiae

Method: X-Ray Diffraction

Resolution: 2.4 Å

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