Open AccessMammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes.
Author(s) -
Oleg Kovalenko,
Annemieke W. Plug,
Thomas Haaf,
David K. Gonda,
Terry Ashley,
David C. Ward,
Charles M. Radding,
Efim I. Golub
Publication year - 1996
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.93.7.2958
Subject(s) - rad51 , ubiquitin conjugating enzyme , biology , synaptonemal complex , schizosaccharomyces pombe , microbiology and biotechnology , ddb1 , homologous recombination , saccharomyces cerevisiae , schizosaccharomyces , genetic recombination , gene , genetics , ubiquitin ligase , homologous chromosome , ubiquitin , recombination
Hsubc9, a human gene encoding a ubiquitin-conjugating enzyme, has been cloned. The 18-kDa HsUbc9 protein is homologous to the ubiquitin-conjugating enzymes Hus5 of Schizosaccharomyces pombe and Ubc9 of Saccharomyces cerevisiae. The Hsubc9 gene complements a ubc9 mutation of S. cerevisiae. It has been mapped to chromosome 16p13.3 and is expressed in many human tissues, with the highest levels in testis and thymus. According to the Ga14 two-hybrid system analysis, HsUbc9 protein interacts with human recombination protein Rad51. A mouse homolog, Mmubc9, encodes an amino acid sequence that is identical to the human protein. In mouse spermatocytes, MmUbc9 protein, like Rad51 protein, localizes in synaptonemal complexes, which suggests that Ubc9 protein plays a regulatory role in meiosis.