Ontology highlight
ABSTRACT:
SUBMITTER: Leung A
PROVIDER: S-EPMC5476585 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Leung Andrew A Jardim Francy-Pesek FP Savic Neda N Monneau Yoan R YR González-Romero Rodrigo R Gudavicius Geoff G Eirin-Lopez Jose M JM Bartke Till T Mackereth Cameron D CD Ausió Juan J Nelson Christopher J CJ
Scientific reports 20170619 1
The nucleoplasmin family of histone chaperones is identified by a pentamer-forming domain and multiple acidic tracts that mediate histone binding and chaperone activity. Within this family, a novel domain organization was recently discovered that consists of an N-terminal nucleoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain. Saccharomyces cerevisiae Fpr4 is one such protein. Here we report that in addition to its known histone prolyl isomerase activities, the F ...[more]