Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation | Zendy

Anastacia R. Parks | Zendy; Jorge C. EscalanteSemerena | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation

Author(s) -

Anastacia R. Parks,

Jorge C. EscalanteSemerena

Publication year - 2020

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.2005296117

Subject(s) - sirtuin , acetylation , nat , biochemistry , acetyltransferase , myristoylation , enzyme , biology , acyltransferase , sirtuin 1 , acetyl coa , chemistry , gene , computer network , downregulation and upregulation , phosphorylation , computer science

Significance N-terminal protein acetylation is poorly understood in bacteria. Herein, we report the identification of an Nα acetyltransferase (NAT) that modulates the activity of a sirtuin deacylase in a human pathogen. This is significant because the alluded enzyme (namedN -acyltransferase A [NatA], formerly YiaC) is a prokaryotic non-Rim–type NAT, and N- terminal acetylation of a bacterial sirtuin has not been reported. Also significant is the fact that NatA affects the metabolism of acetate, a short-chain fatty acid known to play an important role in pathogenesis in the human gut.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research