Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum
Authors: Monica Brown
Amit Sharma
Manickam Yogavel
Anuj Kumar
Jasmita Gill
Alexander G Maier
Melanie Rug
Hassan Belrhali
S K Jain
Journal: Malaria journal (2010)
Discipline: CLINICAL MEDICINE
Keywords: Nucleosome assembly proteins; PfNapS; histone chaperones; Plasmodium falciparum; crystal structure
Affiliations: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Road, New Delhi, 110067, India.

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. 

Retracted: No

PubPeer comments:
  , 
 There is an inadvertent error during composition of the panel. It will be addressed soon. , 
 We have supplied the original images to the journal again as there was an inadvertent error during their composition. We have received the following reply from the journal:  I am sorry that I couldnu2019t be of further help this time and I am sorry if any error occurred on the publisher end during the production of your article . If anyone needs the original images as they were intended to be published please contact us. The original and correct Panel 3 image, Figure 3c-3f, is attached here as well. Apologies for any confusion.  , 
  I am sorry that I couldnu2019t be of further help this time and I am sorry if any error occurred on the publisher end during the production of your article . Amit Sharma, this seems to be a highly surprising response from this indexed and ranked COPE member journal [1]. Could you kindly indicate the person or editor who provided that response. [1] https: malariajournal.biomedcentral.com , 
 #4 First author and myself had contacted the following for this: Joseph.Harrison@springernature.com ,