Publication Date:
2000-01-22
Description:
Although ubiquitinated histones are present in substantial levels in vertebrate cells, the roles they play in specific biological processes and the cellular factors that regulate this modification are not well characterized. Ubiquitinated H2B (uH2B) has been identified in the yeast Saccharomyces cerevisiae, and mutation of the conserved ubiquitination site is shown to confer defects in mitotic cell growth and meiosis. uH2B was not detected in rad6 mutants, which are defective for the ubiquitin-conjugating enzyme Ubc2, thus identifying Rad6 as the major cellular activity that ubiquitinates H2B in yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robzyk, K -- Recht, J -- Osley, M A -- GM40118/GM/NIGMS NIH HHS/ -- R01 GM040118/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):501-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology, Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10642555" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Substitution
;
Histones/*metabolism
;
Ligases/genetics/*metabolism
;
Meiosis
;
Mitosis
;
Mutagenesis, Site-Directed
;
Phenotype
;
Recombinant Fusion Proteins/metabolism
;
Saccharomyces cerevisiae/genetics/*metabolism/physiology
;
*Saccharomyces cerevisiae Proteins
;
Spores, Fungal/physiology
;
Substrate Specificity
;
Ubiquitin-Conjugating Enzymes
;
Ubiquitins/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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