FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1968882280> ?p ?o ?g. }

• W1968882280 endingPage "26215" @default.
• W1968882280 startingPage "26209" @default.
• W1968882280 abstract "The yeast Saccharomyces cerevisiae CDC34 gene encodes a ubiquitin-conjugating enzyme that is required for the cell cycle G1/S transition. We show here that a dominant negative Cdc34 protein is generated by simultaneously replacing both Cys95 and Leu99 with Ser residues. Cys95 is an essential catalytic residue that forms a transient thiol ester with ubiquitin during catalysis, and Leu99 is highly conserved among all known ubiquitin-conjugating enzymes. Mutants that encode either an alanine or a serine at one or both of these two positions are inactive. Of these eight mutants, overexpression of CDC34-C95S,L99S in wild type strains was found to block cell growth. Although cells overexpressing Cdc34-C95S,L99S do not exhibit the characteristic multibudded phenotype of cdc34 temperature-sensitive or null mutants, this blockade is relieved by simultaneous overexpression of wild type Cdc34. Purified Cdc34-C95S,L99S protein can be shown to inhibit in vitro ubiquitination of the Cdc34-specific substrate, Cln2 protein. We suggest that Cdc34-C95S,L99S selectively sequesters a subset of Cdc34 substrates or regulators. These findings have implications for the structure/function relationships of ubiquitin-conjugating enzymes, and suggest a general method for identifying components and substrates of specific ubiquitination pathways of eukaryotes. The yeast Saccharomyces cerevisiae CDC34 gene encodes a ubiquitin-conjugating enzyme that is required for the cell cycle G1/S transition. We show here that a dominant negative Cdc34 protein is generated by simultaneously replacing both Cys95 and Leu99 with Ser residues. Cys95 is an essential catalytic residue that forms a transient thiol ester with ubiquitin during catalysis, and Leu99 is highly conserved among all known ubiquitin-conjugating enzymes. Mutants that encode either an alanine or a serine at one or both of these two positions are inactive. Of these eight mutants, overexpression of CDC34-C95S,L99S in wild type strains was found to block cell growth. Although cells overexpressing Cdc34-C95S,L99S do not exhibit the characteristic multibudded phenotype of cdc34 temperature-sensitive or null mutants, this blockade is relieved by simultaneous overexpression of wild type Cdc34. Purified Cdc34-C95S,L99S protein can be shown to inhibit in vitro ubiquitination of the Cdc34-specific substrate, Cln2 protein. We suggest that Cdc34-C95S,L99S selectively sequesters a subset of Cdc34 substrates or regulators. These findings have implications for the structure/function relationships of ubiquitin-conjugating enzymes, and suggest a general method for identifying components and substrates of specific ubiquitination pathways of eukaryotes." @default.
• W1968882280 created "2016-06-24" @default.
• W1968882280 creator A5026485071 @default.
• W1968882280 creator A5034616035 @default.
• W1968882280 creator A5066867755 @default.
• W1968882280 date "1995-11-01" @default.
• W1968882280 modified "2023-09-26" @default.
• W1968882280 title "Characterization of a Dominant Negative Mutant of the Cell Cycle Ubiquitin-conjugating Enzyme Cdc34" @default.
• W1968882280 cites W1483766000 @default.
• W1968882280 cites W1530194480 @default.
• W1968882280 cites W1548589053 @default.
• W1968882280 cites W1558541683 @default.
• W1968882280 cites W1559325314 @default.
• W1968882280 cites W1566221754 @default.
• W1968882280 cites W1838616807 @default.
• W1968882280 cites W1967390330 @default.
• W1968882280 cites W1978186903 @default.
• W1968882280 cites W1980189056 @default.
• W1968882280 cites W1984367265 @default.
• W1968882280 cites W1985001103 @default.
• W1968882280 cites W2008044453 @default.
• W1968882280 cites W2009073107 @default.
• W1968882280 cites W2013289317 @default.
• W1968882280 cites W2018560829 @default.
• W1968882280 cites W2028622989 @default.
• W1968882280 cites W2041770258 @default.
• W1968882280 cites W2049300709 @default.
• W1968882280 cites W2063856790 @default.
• W1968882280 cites W2070963888 @default.
• W1968882280 cites W2072280454 @default.
• W1968882280 cites W2074126694 @default.
• W1968882280 cites W2076217757 @default.
• W1968882280 cites W2091403769 @default.
• W1968882280 cites W2100837269 @default.
• W1968882280 cites W2106869142 @default.
• W1968882280 cites W2132024812 @default.
• W1968882280 cites W2136776958 @default.
• W1968882280 cites W2138270253 @default.
• W1968882280 cites W2146437721 @default.
• W1968882280 cites W2170939558 @default.
• W1968882280 cites W2171202879 @default.
• W1968882280 cites W2175093343 @default.
• W1968882280 cites W4251683570 @default.
• W1968882280 cites W68591885 @default.
• W1968882280 doi "https://doi.org/10.1074/jbc.270.44.26209" @default.
• W1968882280 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7592826" @default.
• W1968882280 hasPublicationYear "1995" @default.
• W1968882280 type Work @default.
• W1968882280 sameAs 1968882280 @default.
• W1968882280 citedByCount "41" @default.
• W1968882280 countsByYear W19688822802012 @default.
• W1968882280 countsByYear W19688822802013 @default.
• W1968882280 countsByYear W19688822802017 @default.
• W1968882280 countsByYear W19688822802018 @default.
• W1968882280 countsByYear W19688822802021 @default.
• W1968882280 crossrefType "journal-article" @default.
• W1968882280 hasAuthorship W1968882280A5026485071 @default.
• W1968882280 hasAuthorship W1968882280A5034616035 @default.
• W1968882280 hasAuthorship W1968882280A5066867755 @default.
• W1968882280 hasBestOaLocation W19688822801 @default.
• W1968882280 hasConcept C102658986 @default.
• W1968882280 hasConcept C104317684 @default.
• W1968882280 hasConcept C134459356 @default.
• W1968882280 hasConcept C143065580 @default.
• W1968882280 hasConcept C182561583 @default.
• W1968882280 hasConcept C185592680 @default.
• W1968882280 hasConcept C25602115 @default.
• W1968882280 hasConcept C2777576037 @default.
• W1968882280 hasConcept C2779222958 @default.
• W1968882280 hasConcept C55493867 @default.
• W1968882280 hasConcept C86803240 @default.
• W1968882280 hasConceptScore W1968882280C102658986 @default.
• W1968882280 hasConceptScore W1968882280C104317684 @default.
• W1968882280 hasConceptScore W1968882280C134459356 @default.
• W1968882280 hasConceptScore W1968882280C143065580 @default.
• W1968882280 hasConceptScore W1968882280C182561583 @default.
• W1968882280 hasConceptScore W1968882280C185592680 @default.
• W1968882280 hasConceptScore W1968882280C25602115 @default.
• W1968882280 hasConceptScore W1968882280C2777576037 @default.
• W1968882280 hasConceptScore W1968882280C2779222958 @default.
• W1968882280 hasConceptScore W1968882280C55493867 @default.
• W1968882280 hasConceptScore W1968882280C86803240 @default.
• W1968882280 hasIssue "44" @default.
• W1968882280 hasLocation W19688822801 @default.
• W1968882280 hasLocation W19688822802 @default.
• W1968882280 hasOpenAccess W1968882280 @default.
• W1968882280 hasPrimaryLocation W19688822801 @default.
• W1968882280 hasRelatedWork W1987982805 @default.
• W1968882280 hasRelatedWork W1999763554 @default.
• W1968882280 hasRelatedWork W2020599187 @default.
• W1968882280 hasRelatedWork W202451065 @default.
• W1968882280 hasRelatedWork W2060295565 @default.
• W1968882280 hasRelatedWork W2083690210 @default.
• W1968882280 hasRelatedWork W2122628059 @default.
• W1968882280 hasRelatedWork W2133819225 @default.
• W1968882280 hasRelatedWork W2135178058 @default.
• W1968882280 hasRelatedWork W2143057499 @default.
• W1968882280 hasVolume "270" @default.

• next