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http://purl.uniprot.org/citations/1400344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1400344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1400344http://www.w3.org/2000/01/rdf-schema#comment"The MAK3 gene is necessary for propagation of the L-A double-stranded RNA virus of Saccharomyces cerevisiae. MAK3 encodes a protein with substantial homology to the Escherichia coli rimI N-acetyltransferase that acetylates the NH2 terminus of ribosomal protein S18, and shares consensus sequences with a group of N-acetyltransferases. The NH2 terminus of the viral major coat protein encoded by L-A is normally blocked, but we find that it is unblocked in a mak3-1 mutant. L-A virus-encoded proteins produced from a cDNA clone of L-A can encapsidate the L-A (+)-strands in a wild-type host, but not in a mak3-1 mutant strain. The amount of major coat protein found in the particle fraction is reduced greater than 100-fold, and the amount in the total cell extract is reduced 5-10-fold. A modified beta-galactosidase, having as its NH2-terminal the NH2-terminal 13 residues of the L-A-encoded major coat protein, is blocked in a wild-type host, but not in a mak3-1 host. We propose that MAK3 encodes an N-acetyltransferase whose modification of the L-A major coat protein NH2 terminus is essential for viral assembly, and that unassembled coat protein is unstable."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)88697-0"xsd:string
http://purl.uniprot.org/citations/1400344http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)88697-0"xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/author"Wickner R.B."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/author"Wickner R.B."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/author"Tercero J.C."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/author"Tercero J.C."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/pages"20277-20281"xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/pages"20277-20281"xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/title"MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 terminus is necessary for virus particle assembly."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/title"MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 terminus is necessary for virus particle assembly."xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1400344http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1400344http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1400344
http://purl.uniprot.org/citations/1400344http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1400344
http://purl.uniprot.org/citations/1400344http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1400344
http://purl.uniprot.org/citations/1400344http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1400344
http://purl.uniprot.org/uniprot/P32503http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1400344
http://purl.uniprot.org/uniprot/Q03503http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1400344