PMID- 10642555 OWN - NLM STAT- MEDLINE DCOM- 20000207 LR - 20190619 IS - 0036-8075 (Print) IS - 0036-8075 (Linking) VI - 287 IP - 5452 DP - 2000 Jan 21 TI - Rad6-dependent ubiquitination of histone H2B in yeast. PG - 501-4 AB - 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. FAU - Robzyk, K AU - Robzyk K AD - Program in Molecular Biology, Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA. FAU - Recht, J AU - Recht J FAU - Osley, M A AU - Osley MA LA - eng GR - R01 GM040118/GM/NIGMS NIH HHS/United States GR - GM40118/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - United States TA - Science JT - Science (New York, N.Y.) JID - 0404511 RN - 0 (Histones) RN - 0 (Recombinant Fusion Proteins) RN - 0 (Saccharomyces cerevisiae Proteins) RN - 0 (Ubiquitins) RN - EC 2.3.2.23 (RAD6 protein, S cerevisiae) RN - EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes) RN - EC 6.- (Ligases) SB - IM MH - Amino Acid Substitution MH - Histones/*metabolism MH - Ligases/genetics/*metabolism MH - Meiosis MH - Mitosis MH - Mutagenesis, Site-Directed MH - Phenotype MH - Recombinant Fusion Proteins/metabolism MH - Saccharomyces cerevisiae/genetics/*metabolism/physiology MH - *Saccharomyces cerevisiae Proteins MH - Spores, Fungal/physiology MH - Substrate Specificity MH - Ubiquitin-Conjugating Enzymes MH - Ubiquitins/*metabolism EDAT- 2000/01/22 00:00 MHDA- 2000/01/22 00:01 CRDT- 2000/01/22 00:00 PHST- 2000/01/22 00:00 [pubmed] PHST- 2000/01/22 00:01 [medline] PHST- 2000/01/22 00:00 [entrez] AID - 8193 [pii] AID - 10.1126/science.287.5452.501 [doi] PST - ppublish SO - Science. 2000 Jan 21;287(5452):501-4. doi: 10.1126/science.287.5452.501.