In:
Angewandte Chemie International Edition, Wiley, Vol. 61, No. 30 ( 2022-07-25)
Abstract:
Structurally diverse acylations have been identified as post‐translational modifications (PTMs) on histone lysine residues, but their functions and regulations remain largely unknown. Interestingly, in nature, a lysine acylation analog, pyrrolysine, is introduced as a co‐translational modification (CTM) through genetic encoding. To explore this alternative life form, we created a model organism Saccharomyces cerevisiae containing site‐specific lysine CTMs (acetyl‐lysine, crotonyl‐lysine, or another synthetic analog) at histone H3K56 using non‐canonical amino acid mutagenesis to afford a chemically modified nucleosome in lieu of their own in vivo . We further demonstrated that acetylation of histone H3K56 partly tends to provide a more favorable chromatin environment for DNA repair in yeast compared to crotonylation and crosstalk with other PTMs differently. This study provides a potentially universal approach to decipher the consequences of different histone lysine PTMs in eukaryotes.
Type of Medium:
Online Resource
ISSN:
1433-7851
,
1521-3773
DOI:
10.1002/anie.202205570
Language:
English
Publisher:
Wiley
Publication Date:
2022
detail.hit.zdb_id:
2011836-3
detail.hit.zdb_id:
123227-7