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Gene Review

NAT1  -  Nat1p

Saccharomyces cerevisiae S288c

Synonyms: AAA1, Amino-terminal, alpha-amino, acetyltransferase 1, D2720, N-terminal acetyltransferase A complex subunit NAT1, NAA15, ...
 
 
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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

References

  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]
 
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