The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

NAT1  -  Nat1p

Saccharomyces cerevisiae S288c

Synonyms: AAA1, Amino-terminal, alpha-amino, acetyltransferase 1, D2720, N-terminal acetyltransferase A complex subunit NAT1, NAA15, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on NAT1

  • For all three propeptide-deleted subunits, activity of the affected catalytic center is fully restored when the Nat1-Ard1 Nalpha-acetyltransferase is mutated [1].
  • Regions of this gene, NAT1, and the chloramphenicol acetyltransferase genes of bacteria have limited but significant homology [2].
  • A gene from Saccharomyces cerevisiae has been mapped, cloned, sequenced and shown to encode a catalytic subunit of an N-terminal acetyltransferase [2].
  • 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 [2].
  • Our analysis shows that an AAA1 hydrolysis mutant blocks dynein function, whereas a triple AAA2/3/4 hydrolysis mutant does not, suggesting that nucleotide binding is required at only one site [3].

Biological context of NAT1

  • These results suggest that NAT1 and ARD1 proteins function together to catalyze the N-terminal acetylation of a subset of yeast proteins [2].
  • Temperature sensitivity and derepression of silent mating type loci caused by Delta nat1 or Delta ard1 were partially suppressed by overexpression of SSB1 [4].
  • The determined nucleotide sequence was identical to that reported for NAT1 [5].
  • DNA blot hybridizations of genomic and chromosomal DNA reveal that the gene (so-called AAA1, amino-terminal, alpha-amino, acetyltransferase) is present as a single copy located on chromosome IV [6].
  • NARG2 and NARG3 appear to be novel, while NARG1 is the mammalian homologue of a yeast N-terminal acetyltransferase that regulates entry into the G(o) phase of the cell cycle [7].

Anatomical context of NAT1


Associations of NAT1 with chemical compounds

  • However, the chymotrypsin-like activity in the absence of sodium dodecyl sulfate was slightly higher in the nat1 mutant than in the normal strain [8].
  • A direct comparison revealed that Nat1p required longer nascent polypeptides for interaction than NAC and Ssb1/2p [4].
  • Using a mutant of Saccharomyces cerevisiae defective in the NAT1 gene, that encodes one of the NH2-terminal acetyltransferases, we have identified 14 ribosomal proteins whose electrophoretic mobility at pH 5.0 suggests they carry an additional charge, presumably due to the lack of NH2-terminal acetylation [9].

Other interactions of NAT1


  1. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. Arendt, C.S., Hochstrasser, M. EMBO J. (1999) [Pubmed]
  2. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. Mullen, J.R., Kayne, P.S., Moerschell, R.P., Tsunasawa, S., Gribskov, M., Colavito-Shepanski, M., Grunstein, M., Sherman, F., Sternglanz, R. EMBO J. (1989) [Pubmed]
  3. Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae. Reck-Peterson, S.L., Vale, R.D. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Gautschi, M., Just, S., Mun, A., Ross, S., Rücknagel, P., Dubaquié, Y., Ehrenhofer-Murray, A., Rospert, S. Mol. Cell. Biol. (2003) [Pubmed]
  5. Hamster monomorphic arylamine N-acetyltransferase: expression in Escherichia coli and purification. Bergstrom, C.P., Wagner, C.R., Ann, D.K., Hanna, P.E. Protein Expr. Purif. (1995) [Pubmed]
  6. Molecular cloning and sequencing of a cDNA encoding N alpha-acetyltransferase from Saccharomyces cerevisiae. Lee, F.J., Lin, L.W., Smith, J.A. J. Biol. Chem. (1989) [Pubmed]
  7. N-methyl-D-aspartate receptors regulate a group of transiently expressed genes in the developing brain. Sugiura, N., Patel, R.G., Corriveau, R.A. J. Biol. Chem. (2001) [Pubmed]
  8. N(alpha)-acetylation and proteolytic activity of the yeast 20 S proteasome. Kimura, Y., Takaoka, M., Tanaka, S., Sassa, H., Tanaka, K., Polevoda, B., Sherman, F., Hirano, H. J. Biol. Chem. (2000) [Pubmed]
  9. NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. Takakura, H., Tsunasawa, S., Miyagi, M., Warner, J.R. J. Biol. Chem. (1992) [Pubmed]
  10. The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. Caesar, R., Blomberg, A. J. Biol. Chem. (2004) [Pubmed]
WikiGenes - Universities