Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum.

ABSTRACT:

Background

Nucleosome assembly proteins (NAPs) are histone chaperones that are crucial for the shuttling and incorporation of histones into nucleosomes. NAPs participate in the assembly and disassembly of nucleosomes thus contributing to chromatin structure organization. The human malaria parasite Plasmodium falciparum contains two nucleosome assembly proteins termed PfNapL and PfNapS.

Methods

Three-dimensional crystal structure of PfNapS has been determined and analysed. Gene knockout and localization studies were also performed on PfNapS using transfection studies. Fluorescence spectroscopy was performed to identify histone-binding sites on PfNapS. Extensive sequence and structural comparisons were done with the crystal structures available for NAP/SET family of proteins.<

SUBMITTER: Gill J 

PROVIDER: S-EPMC2873526 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature