In:
Angewandte Chemie, Wiley, Vol. 134, No. 30 ( 2022-07-25)
Kurzfassung:
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.
Materialart:
Online-Ressource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v134.30
DOI:
10.1002/ange.202205570
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2022
ZDB Id:
505868-5
ZDB Id:
506609-8
ZDB Id:
514305-6
ZDB Id:
505872-7
ZDB Id:
1479266-7
ZDB Id:
505867-3
ZDB Id:
506259-7