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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

Gholson J Lyon  1
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.

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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).
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Comment on

References

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