From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases
- PMID: 31269458
- PMCID: PMC7313478
- DOI: 10.1016/j.str.2019.06.002
From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases
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.
Copyright © 2019 Elsevier Ltd. All rights reserved.
Figures

Comment on
-
Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.Structure. 2019 Jul 2;27(7):1057-1070.e4. doi: 10.1016/j.str.2019.04.014. Epub 2019 May 30. Structure. 2019. PMID: 31155310 Free PMC article.
References
-
- 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
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases