Mechanistic basis for the role of acidic tail of Rad6 (ubiquitin-conjugating enzyme) in Bre1 (E3 ligase) mediated recognition of histones in Saccharomyces cerevisiae
Year: 2024
Type: conference-abstract
Abstract: E2 Rad6 and E3 Bre1 are indispensable for H2B K123 monoubiquitination in budding yeast however, the mechanistic basis for the fidelity of the ubiquitination reaction was not clear. The present study reveals two important findings: (i) ) the involvement of Rad6 acidic tail and a positive charged surface of histone H2B in E2-NCP recognition prior to ubiquitin transfer, and (ii) direct interaction of Bre1 RBD with Rad6 prevents promiscuous ubiquitin transfer to histone lysine residues, allowing site-specific monoubiquitination in conjunction with the RING domain Conclusion Results
Source: European Peptide Symposium (EPS)
Institutions: Jamia Hamdard, Johns Hopkins University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W4403190745