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- W158285355 abstract "Research Article1 July 1989free access Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. J. R. Mullen J. R. Mullen Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author P. S. Kayne P. S. Kayne Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author R. P. Moerschell R. P. Moerschell Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author S. Tsunasawa S. Tsunasawa Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Gribskov M. Gribskov Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Colavito-Shepanski M. Colavito-Shepanski Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Grunstein M. Grunstein Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author F. Sherman F. Sherman Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author R. Sternglanz R. Sternglanz Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author J. R. Mullen J. R. Mullen Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author P. S. Kayne P. S. Kayne Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author R. P. Moerschell R. P. Moerschell Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author S. Tsunasawa S. Tsunasawa Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Gribskov M. Gribskov Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Colavito-Shepanski M. Colavito-Shepanski Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author M. Grunstein M. Grunstein Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author F. Sherman F. Sherman Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author R. Sternglanz R. Sternglanz Department of Biochemistry, State University of New York, Stony Brook 11794. Search for more papers by this author Author Information J. R. Mullen1, P. S. Kayne1, R. P. Moerschell1, S. Tsunasawa1, M. Gribskov1, M. Colavito-Shepanski1, M. Grunstein1, F. Sherman1 and R. Sternglanz1 1Department of Biochemistry, State University of New York, Stony Brook 11794. The EMBO Journal (1989)8:2067-2075https://doi.org/10.1002/j.1460-2075.1989.tb03615.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A gene from Saccharomyces cerevisiae has been mapped, cloned, sequenced and shown to encode a catalytic subunit of an N-terminal acetyltransferase. Regions of this gene, NAT1, and the chloramphenicol acetyltransferase genes of bacteria have limited but significant homology. A nat1 null mutant is viable but exhibits a variety of phenotypes, including reduced acetyltransferase activity, derepression of a silent mating type locus (HML) and failure to enter G0. All these phenotypes are identical to those of a previously characterized mutant, ard1. NAT1 and ARD1 are distinct genes that encode proteins with no obvious similarity. Concomitant overexpression of both NAT1 and ARD1 in yeast causes a 20-fold increase in acetyltransferase activity in vitro, whereas overexpression of either NAT1 or ARD1 alone does not raise activity over basal levels. A functional iso-1-cytochrome c protein, which is N-terminally acetylated in a NAT1 strain, is not acetylated in an isogenic nat1 mutant. At least 20 other yeast proteins, including histone H2B, are not N-terminally acetylated in either nat1 or ard1 mutants. These results suggest that NAT1 and ARD1 proteins function together to catalyze the N-terminal acetylation of a subset of yeast proteins. Previous ArticleNext Article Volume 8Issue 71 July 1989In this issue RelatedDetailsLoading ..." @default.
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- W158285355 title "Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast." @default.
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- W158285355 doi "https://doi.org/10.1002/j.1460-2075.1989.tb03615.x" @default.
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