Document Detail


Tandemly repeated genes encode nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii.
MedLine Citation:
PMID:  7961894     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The obligate intracellular parasite Toxoplasma gondii produces a nucleoside triphosphate hydrolase (NTPase) (nucleoside-triphosphatase, EC 3.6.1.15) activable by dithiol-containing compounds. We have isolated the genomic DNA for the NTPase from the RH strain of Toxoplasma and determined the nucleotide sequence of three tandemly arranged open reading frames termed NTP1, NTP2, and NTP3. We have also isolated and sequenced cDNAs for NTP1 and NTP3; no cDNA for NTP2 was obtained. The two cDNA clones encode proteins that are more than 97% identical at the amino acid level but significantly differ within two small domains, indicating the presence of NTPase isoforms. Both possess N-terminal signal sequences and two regions with partial homology to certain known ATP binding motifs: the glycine-rich loop common to many ATP binding proteins and the beta-phosphate binding domain found in the hexokinase-actin-hsp70 family. Antiserum against a NTP1-fusion protein immunoprecipitated NTPase activity from extracellular parasites that was increased in activity by treatment with dithiothreitol, confirming the identity of the cloned genes. By immunofluorescence, the NTPase is located in vesicular structures within the parasite, and in infected cells it is secreted into the vacuolar space and becomes partially associated with the parasitophorous vacuolar membrane. Since the vacuolar membrane is freely permeable to small molecules of < 1300 Da, host cell ATP may serve as a substrate for the NTPase and supply the energy for parasite-directed processes in the vacuolar space.
Authors:
D Bermudes; K R Peck; M A Afifi; C J Beckers; K A Joiner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  269     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1994 Nov 
Date Detail:
Created Date:  1994-12-19     Completed Date:  1994-12-19     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  29252-60     Citation Subset:  IM    
Affiliation:
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06520-8022.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/L39077;  U14322;  U14323;  U14324
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MeSH Terms
Descriptor/Qualifier:
Acid Anhydride Hydrolases / genetics*
Amino Acid Sequence
Animals
Antibodies, Protozoan / immunology
Base Sequence
DNA, Protozoan
Dithiothreitol / pharmacology
Enzyme Activation
Genes, Protozoan*
Mice
Molecular Sequence Data
Multigene Family
Nucleoside-Triphosphatase
Precipitin Tests
Recombinant Fusion Proteins / immunology
Sequence Homology, Amino Acid
Toxoplasma / enzymology,  genetics*,  physiology
Vacuoles / enzymology
Grant Support
ID/Acronym/Agency:
R01 A1 30060//PHS HHS; UOI AI 31808/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Antibodies, Protozoan; 0/DNA, Protozoan; 0/Recombinant Fusion Proteins; 3483-12-3/Dithiothreitol; EC 3.6.-/Acid Anhydride Hydrolases; EC 3.6.1.15/Nucleoside-Triphosphatase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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