Document Detail


Plasmodium falciparum Tudor Staphylococcal Nuclease interacting proteins suggest its role in nuclear as well as splicing processes.
MedLine Citation:
PMID:  20713134     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Tudor Staphylococcal Nuclease (p100 or SND1), a member of the micronuclease family is a multifunctional protein that plays a key role(s) in transcription and splicing processes in many eukaryotic cells. PfTudor-SN, a Plasmodium homolog of the human p100 protein is a structurally conserved protein; however molecular details of its function are not yet understood. Our previous studies have shown that PfTudor-SN binds RNA and it is possible to selectively inhibit parasite growth by PfTudor-SN specific drugs. In the present study, we identified the molecular interactions between Plasmodium falciparum Tudor-SN and twelve Plasmodium proteins such as Histone h2A, SPT2 (a transcriptional regulator), a Cold-shock DNA binding protein in a bacterial two-hybrid screen. To get further insight into some of these interactions, we mapped the interaction domain in PfTudor-SN protein using the yeast two-hybrid system. Of these proteins, Plasmodium N-methyl-d-aspartate receptor associated protein, PfUbiquitin conjugating enzyme and Cold-shock DNA binding protein showed interaction with the SN domains of PfTudor-SN. Immuno-localization studies of the interacting proteins showed their presence predominantly in the nucleus, which inevitably suggests the molecular interactions between these proteins and PfTudor-SN. Furthermore, we also identified a molecular interaction between the Tudor domain of PfTudor-SN protein and Plasmodium spliceosomal Sm protein, PfSmD1 advocating the role of PfTudor-SN in the spliceosome assembly. Together, these results suggest multiple role(s) for PfTudor-SN protein mainly in nuclear and splicing processes at asexual blood stages of the malaria parasite.
Authors:
Manzar J Hossain; Reshma Korde; Prashant K Singh; Shivani Kanodia; Ravi Ranjan; Geeta Ram; Gaganjot Singh Kalsey; Rita Singh; Pawan Malhotra
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-08-14
Journal Detail:
Title:  Gene     Volume:  468     ISSN:  1879-0038     ISO Abbreviation:  Gene     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-09-27     Completed Date:  2010-10-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7706761     Medline TA:  Gene     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  48-57     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier B.V. All rights reserved.
Affiliation:
Malaria Group, International Centre for Genetic Engineering and Biotechnology, New Delhi-110067, India.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Blotting, Western
Cell Nucleus / enzymology*,  genetics*
Gene Library
Immunoprecipitation
Life Cycle Stages
Micrococcal Nuclease / chemistry,  metabolism*
Models, Molecular
Molecular Sequence Data
Peptides / chemistry
Plasmodium falciparum / enzymology*,  genetics*,  growth & development
Protein Binding
Protein Structure, Tertiary
Protein Transport
Protozoan Proteins / chemistry,  metabolism*
RNA Splicing / physiology*
Spliceosomes / metabolism
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Peptides; 0/Protozoan Proteins; EC 3.1.31.1/Micrococcal Nuclease

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