Bre1 mediates the ubiquitination of histone H2B by regulating Lge1 stability

Histone H2B ubiquitination mediated by the Rad6/Bre1 complex is crucial for regulating the stability and reassembly of the nucleosome. To understand the regulatory mechanisms of H2B ubiquitination, we explored proteins related to the Rad6/Bre1 complex. Interestingly, we observed that the stability o...

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Bibliographic Details
Published inFEBS letters Vol. 592; no. 9; pp. 1565 - 1574
Main Authors Kim, Jueun, An, Yu‐Kyoung, Park, Shinae, Lee, Jung‐Shin
Format Journal Article
LanguageEnglish
Published England 01.05.2018
Subjects
Bre1
H2B ubiquitination
Histones - metabolism
Lge1 stability
Protein Stability
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Transcription Factors - metabolism
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
H2B ubiquitination
Lge1 stability
Bre1
Saccharomyces cerevisiae
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Summary:Histone H2B ubiquitination mediated by the Rad6/Bre1 complex is crucial for regulating the stability and reassembly of the nucleosome. To understand the regulatory mechanisms of H2B ubiquitination, we explored proteins related to the Rad6/Bre1 complex. Interestingly, we observed that the stability of Lge1, reported to be a cofactor of Bre1, is greatly reduced in the absence of Bre1. The stability of Lge1 did require the middle fragment of Bre1 containing a coiled‐coil structure, but not its E3 ligase activity. Additionally, we found that Lge1 is involved in the ‘writing’ step of H2B ubiquitination. Our data suggest that Bre1 mediates H2B ubiquitination more precisely by maintaining the stability of Lge1 as well as through its role as a known E3 ligase.
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ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13049