Linda G. Beatty

TL;DR: This work used massively diverse combinatorial libraries of ubiquitin variants to develop inhibitors of four deubiquitinases (DUBs) and analyzed the DUB-inhibitor complexes with crystallography to report a method to target the myriad enzymes that govern ubiquitination of protein substrates.

TL;DR: It is demonstrated that FLP introduces single- and double-strand breaks into the substrate DNA and binding to mutant sites and half-sites demonstrates that the third symmetry element is not important for binding and cleavage by the FLP protein.

TL;DR: It is shown that the CTCF protein can be posttranslationally modified by the small ubiquitin-like protein SUMO, and two major sites of SUMOylation in the protein are identified, both in vivo and in vitro.

TL;DR: The existence of insulators in H19 DMR is confirmed and two novel insulator sequences are discovered in the IGF2 gene, and binding of CTCF protein in vitro is demonstrated to all the insulator and silencer sequences that are detected.

TL;DR: On the basis of the behavior of various FLP target sequences in the gel-binding assay, a model describing the steps that lead to the formation of a stable FLP-DNA complex is proposed.