Ontology highlight
ABSTRACT:
SUBMITTER: Ludwigsen J
PROVIDER: S-EPMC5305211 | biostudies-literature | 2017 Jan
REPOSITORIES: biostudies-literature
Ludwigsen Johanna J Pfennig Sabrina S Singh Ashish K AK Schindler Christina C Harrer Nadine N Forné Ignasi I Zacharias Martin M Mueller-Planitz Felix F
eLife 20170121
ISWI-family nucleosome remodeling enzymes need the histone H4 N-terminal tail to mobilize nucleosomes. Here we mapped the H4-tail binding pocket of ISWI. Surprisingly the binding site was adjacent to but not overlapping with the docking site of an auto-regulatory motif, AutoN, in the N-terminal region (NTR) of ISWI, indicating that AutoN does not act as a simple pseudosubstrate as suggested previously. Rather, AutoN cooperated with a hitherto uncharacterized motif, termed AcidicN, to confer H4-t ...[more]