Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Sep 8;46(21):11251–11261. doi: 10.1093/nar/gky801

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 4. — The N-terminus of Dot1 is necessary and sufficient to promote H2Bub1. (A) Schematic representation of the yeast Dot1 protein and different mutants used in this study. (B) Deletion of the Dot1 N-terminal part (DOT1-ΔN-1) abolished the effect of Dot1 on H2Bub1 without altering the expression level of constitutively overexpressed Dot1. (C) Inducible overexpression in galactose media of the N-terminus alone (Dot1-ΔC) was sufficient to promote H2Bub1. The lane with DOT1-ΔC-terminal originates from the same blot. The pan-Dot1 antibody was raised against full-length Dot1, but preferentially recognizes the N-terminus (Supplementary Figure S4). (D) Quantification of the immunoblot shown in (C) (mean and individual data points of two biological replicates). (E) A model for the mutual crosstalk between Dot1 and H2Bub. The catalysis of (de)modifying reactions is indicated by a black arrow or bar-headed line. Stimulation is visualized by white arrows. In short, H2BK123ub1 promotes H3K79 methylation by Dot1 and the N-terminus of Dot1 promotes ubiquitination of H2BK123. The latter stimulation is independent of deubiquitination by Upb8 and the recruitment of Bre1/Rad6 by the Paf complex, and is thus likely to directly act on ubiquitination by Bre1.