Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum
- Author(s)
- Gill, J; Kumar, A; Yogavel, M; Belrhali, H; Jain, SK; Rug, M; Brown, M; Maier, AG; Sharma, A;
- Journal Title
- MALARIA JOURNAL
- Publication Type
- Journal Article
- 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. Results: Crystal structure of PfNapS shares structural similarity with previous structures from NAP/SET family. Failed attempts to knock-out the gene for PfNapS from malaria parasite suggest essentiality in the parasite. GFP-fused PfNapS fusion protein targeting indicates cellular localization of PfNapS in the parasite nucleus. Fluorescence spectroscopy data suggest that PfNapS interacts with core histones (tetramer, octamer, H3, H4, H2A and H2B) at a different site from its interaction with linker histone H1. This analysis illustrates two regions on the PfNapS dimer as the possible sites for histone recognition. Conclusions: This work presents a thorough analysis of the structural, functional and regulatory attributes of PfNapS from P. falciparum with respect to previously studied histone chaperones.
- Publisher
- BIOMED CENTRAL LTD
- Keywords
- INFECTED HUMAN ERYTHROCYTES; CRYSTAL-STRUCTURE; DNA-REPLICATION; CHAPERONE; MALARIA; NAP1; ACRYLODAN; REPAIR; MODEL; VPS75
- Research Division(s)
- Infection And Immunity
- Publisher's Version
- https://doi.org/10.1186/1475-2875-9-90
- Open Access at Publisher's Site
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2873526/- Terms of Use/Rights Notice
- © 2010 Gill et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Creation Date: 2010-04-08 12:00:00