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Literature summary for 2.3.2.23 extracted from

  • Shukla, P.K.; Bissell, J.E.; Kumar, S.; Pokhrel, S.; Palani, S.; Radmall, K.S.; Obidi, O.; Parnell, T.J.; Brasch, J.; Shrieve, D.C.; Chandrasekharan, M.B.
    Structure and functional determinants of Rad6-Bre1 subunits in the histone H2B ubiquitin-conjugating complex (2023), Nucleic Acids Res., 51, 2117-2136.
    View publication on PubMed
Search for more literature for 2.3.2.23

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of Rad6 and the non-RING domain N-terminal region of Bre1 shows an asymmetric homodimer of Bre1 contacting a conserved loop on the Rad6 backside Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D45K mutation strongly reduces Bre1 binding, causes severe in vivo reduction in H2Bub1 and a telomeric silencing defect Saccharomyces cerevisiae
E49K interaction interface mutant, protein does not associate with Bre1. Steady-state levels ofH2Bub1 andH3K4me3 are reduced in mutant strains Saccharomyces cerevisiae
G42A mutation increases Rad6-Bre1 interaction and leads to a decrease in H2Bub1 levels Saccharomyces cerevisiae
P43L interaction interface mutant, binds Bre1 5fold more tightly than native Rad6 in vitro, shows reduced chromatin association of Bre1 and reduced levels of H2Bub1 in vivo Saccharomyces cerevisiae
P43L/E49K interaction interface mutant, protein does not associate with Bre1 Saccharomyces cerevisiae
T46A mutation increases Rad6-Bre1 interaction and leads to a decrease in H2Bub1 levels Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P06104
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Synonyms

Synonyms Comment Organism
Rad6
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information Rad6 and the non-RING domain N-terminal region of Bre1 form an asymmetric homodimer of Bre1 contacting a conserved loop on the Rad6 backside, distant from the Rad6 catalytic site. Mutations that impair telomeric silencing are located at the contact site, which is important for for the Rad6-Bre1 interaction, chromatin-binding dynamics, H2Bub1 formation and gene expression. The non-RING N-terminal region of Bre1 is sufficient to confer nucleosome binding ability to Rad6 in vitro Saccharomyces cerevisiae