A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)
Open Access
- 1 January 2009
- journal article
- Published by Springer Nature in BMC Biochemistry
- Vol. 10 (1) , 15
- https://doi.org/10.1186/1471-2091-10-15
Abstract
Protein acetylation is among the most common protein modifications. The two major types are post-translational Nε-lysine acetylation catalyzed by KATs (Lysine acetyltransferases, previously named HATs (histone acetyltransferases) and co-translational Nα-terminal acetylation catalyzed by NATs (N-terminal acetyltransferases). The major NAT complex in yeast, NatA, is composed of the catalytic subunit Naa10p (N alpha acetyltransferase 10 protein) (Ard1p) and the auxiliary subunit Naa15p (Nat1p). The NatA complex potentially acetylates Ser-, Ala-, Thr-, Gly-, Val- and Cys- N-termini after Met-cleavage. In humans, the homologues hNaa15p (hNat1) and hNaa10p (hArd1) were demonstrated to form a stable ribosome associated NAT complex acetylating NatA type N-termini in vitro and in vivo.Keywords
This publication has 36 references indexed in Scilit:
- Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humansProceedings of the National Academy of Sciences, 2009
- Implication of human N-α-acetyltransferase 5 in cellular proliferation and carcinogenesisOncogene, 2008
- Human Arrest Defective 1 Acetylates and Activates β-Catenin, Promoting Lung Cancer Cell ProliferationCancer Research, 2006
- Analysis of ARD1 Function in Hypoxia Response Using Retroviral RNA InterferenceJournal of Biological Chemistry, 2005
- An Evolutionarily Conserved N-terminal Acetyltransferase Complex Associated with Neuronal DevelopmentJournal of Biological Chemistry, 2003
- The characterization of free, cytoskeletal and membrane-bound polysomes in Krebs II ascites and 3T3 cellsMolecular and Cellular Biochemistry, 1991
- The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathwaysCell, 1985
- Structures of N‐terminally acetylated proteinsEuropean Journal of Biochemistry, 1985
- A comparison of the turnover of alpha-N-acetylated and nonacetylated mouse L-cell proteins.Journal of Biological Chemistry, 1979
- Acetylation of protein N-terminal amino groups structural observations on α-amino acetylated proteinsJournal of Theoretical Biology, 1975