ArticleThe Journal of biological chemistry2009
Crystal structure of malaria parasite nucleosome assembly protein: distinct modes of protein localization and histone recognition.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Association of NAP1L1 polymorphism with clinicopathological progression in oral squamous cell carcinoma.Journal of Cancer · 2026Article
- Nucleosome assembly protein-like 1 degradation-dependent novel cardioprotection mechanism of Wnt2 against ischemia‒reperfusion injury.Signal transduction and targeted therapy · 2025Article
- Chemo-proteomics in antimalarial target identification and engagement.Medicinal research reviews · 2023Review
- Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones.Epigenetics & chromatin · 2022Review
- PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022Article
- NAP1L1 interacts with hepatoma-derived growth factor to recruit c-Jun inducing breast cancer growth.Cancer cell international · 2021Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Inverse docking based screening and identification of protein targets for Cassiarin alkaloids againstSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- Development of a Photo-Cross-Linkable Diaminoquinazoline Inhibitor for Target Identification in Plasmodium falciparum.ACS infectious diseases · 2018Article
- An Integrated Approach to Explore Composition and Dynamics of Cholesterol-rich Membrane Microdomains in Sexual Stages of Malaria Parasite.Molecular & cellular proteomics : MCP · 2017Article
- Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases.Scientific reports · 2017Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- Inhibition of protein synthesis and malaria parasite development by drug targeting of methionyl-tRNA synthetases.Antimicrobial agents and chemotherapy · 2015Article
- Evolutionary and structural annotation of disease-associated mutations in human aminoacyl-tRNA synthetases.BMC genomics · 2014Article
- Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase.Journal of structural and functional genomics · 2014Article
- Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.Journal of structural and functional genomics · 2014Article
- Large multimeric assemblies of nucleosome assembly protein and histones revealed by small-angle X-ray scattering and electron microscopy.The Journal of biological chemistry · 2012Article
- Basic concepts of epigenetics: impact of environmental signals on gene expression.Epigenetics · 2012Review
- Experimentally controlled downregulation of the histone chaperone FACT in Plasmodium berghei reveals that it is critical to male gamete fertility.Cellular microbiology · 2011Article
- The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.Molecular cell · 2011Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleosome assembly proteins (NAPs) are histone chaperones that are essential for the transfer and incorporation of histones into nucleosomes. NAPs participate in assembly and disassembly of nucleosomes and in chromatin structure organization. Human malaria parasite Plasmodium falciparum contains two nucleosome assembly proteins termed PfNapL and PfNapS. To gain structural insights into the mechanism of NAPs, we have determined and analyzed the crystal structure of PfNapL at 2.3 A resolution. PfNapL, an ortholog of eukaryotic NAPs, is dimeric in nature and adopts a characteristic fold seen previously for yeast NAP-1 and Vps75 and for human SET/TAF-1b (beta)/INHAT. The PfNapL monomer is comprised of domain I, containing a dimerization alpha-helix, and a domain II, composed of alpha-helices and a beta-subdomain. Structural comparisons reveal that the "accessory domain," which is inserted between the domain I and domain II in yeast NAP-1 and other eukaryotic NAPs, is surprisingly absent in PfNapL. Expression of green fluorescent protein-tagged PfNapL confirmed its exclusive localization to the parasite cytoplasm. Attempts to disrupt the PfNapL gene were not successful, indicating its essential role for the malaria parasite. A detailed analysis of PfNapL structure suggests unique histone binding properties. The crucial structural differences observed between parasite and yeast NAPs shed light on possible new modes of histone recognition by nucleosome assembly proteins.
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