Active destruction of defective ribosomes by a ubiquitin ligase involved in DNA repair.
Progression of DNA replication forks through damaged DNA requires a ubiquitin ligase comprised of the cullin Rtt101, the RING finger protein Hrt1, and the adaptor protein Mms1. Rtt101 and Mms1 were implicated recently by Fujii and colleagues (pp. 963-974) in the degradation of catalytically inactive mutant 25S ribosomal RNAS (rRNAs) in mature 60S ribosomal subunits, a process that requires ubiquitin and is accompanied by ubiquitination of 60S components. It now seems likely that the same ubiquitin ligase is enlisted to deal with defective rRNA and damaged DNA.
Hinnebusch
Alan G
AG
Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA. ahinnebusch@nih.gov
D004249:DNA Damage / Q000235:genetics; D004260:DNA Repair; D009154:Mutation / Q000235:genetics; D054683:Ribosome Subunits, Large, Eukaryotic / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism*
D043743:Ubiquitin-Protein Ligase Complexes