Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2019 Jul 2;27(7):1053-1055.
doi: 10.1016/j.str.2019.06.002.

From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases

Affiliations
Comment

From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases

Gholson J Lyon. Structure. .

Abstract

In this issue of Structure, Deng et al. (2019) determine the structure of the yeast N-terminal acetyltransferases Naa10 and Naa50 in complex with Naa15 and demonstrate that Naa50 has negligible catalytic activity on its own but modulates Naa10/Naa15. This study provides insights into mechanisms involving amino-terminal acetylation of proteins.

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
The co-translational N-terminal protein modification process. As soon as the nascent polypeptide chain emerges from the ribosome exit tunnel, the initiator methionine (iMet) is cleaved by methionine aminopeptidases (MetAPs) when the second amino acid is small and uncharged. The new N-termini can get acetylated by NatA, which comprises the catalytic Naa10 and the auxiliary subunit Naa15, with or without HYPK. The majority of cytosolic proteins fall into this category. If the iMet is not processed, NTA can be carried out by NatB (composed of Naa20 and Naa25), NatC (Naa30, Naa35, Naa38), NatE (Naa50 and Naa15), NatF (Naa60), or NatG (Naa70).

Comment on

References

    1. Aksnes H, Ree R, and Arnesen T (2019). Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases. Mol. Cell 73, 1097–1114. - PMC - PubMed
    1. Cheng H, Gottlieb L, Marchi E, Kleyner R, Bhardwaj P, Rope AF, Rosenheck S, Moutton S, Philippe C, Eyaid W, et al. (2019). Phenotypic and biochemical analysis of an international cohort of individuals with variants in NAA10 and NAA15. Hum. Mol. Genet doi: 10.1093/hmg/ddz111. [Epub ahead of print]. - DOI - PMC - PubMed
    1. Deng S, Magin RS, Wei X, Pan B, Petersson EJ, and Marmorstein R (2019). Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Structure. in press. - PMC - PubMed
    1. Friedmann DR, and Marmorstein R (2013). Structure and mechanism of non-histone protein acetyltransferase enzymes. FEBS J. 280, 5570–5581. - PMC - PubMed
    1. Gautschi M, Just S, Mun A, Ross S, Rucknagel P, Dubaquie Y, Ehrenhofer-Murray A, and Rospert S (2003). The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol 23, 7403–7414. - PMC - PubMed

MeSH terms

Substances

LinkOut - more resources