From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases

Gholson J Lyon

doi:10.1016/j.str.2019.06.002

From Molecular Understanding to Organismal Biology of N-Terminal Acetyltransferases

Structure. 2019 Jul 2;27(7):1053-1055. doi: 10.1016/j.str.2019.06.002.

Author

Gholson J Lyon¹

Affiliation

¹ Institute for Basic Research in Developmental Disabilities (IBR), Staten Island, NY 10314, USA; Biology PhD Program, The Graduate Center, The City University of New York, NY 10016, USA. Electronic address: gholsonjlyon@gmail.com.

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.

Publication types

Comment

MeSH terms

Acetylation
N-Terminal Acetyltransferase A*
N-Terminal Acetyltransferase E*
N-Terminal Acetyltransferases
Protein Processing, Post-Translational

Substances

N-Terminal Acetyltransferase A
N-Terminal Acetyltransferase E
N-Terminal Acetyltransferases

Grants and funding

R35 GM133408/GM/NIGMS NIH HHS/United States