Document Detail


Evidence of nucleotidyl phosphatase activity associated with core protein sigma A of avian reovirus S1133.
MedLine Citation:
PMID:  11886258     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Both avian reovirus core protein sigma A purified from virus-infected cell extracts and the purified bacterially expressed protein sigma A (e sigma A) were characterized for their nucleoside triphosphate (NTP) hydrolysis activity by thin-layer chromotography. Protein sigma A from both preparations has a nonspecific nucleotidyl phosphatase activity that hydrolyzes four types of NTP to their corresponding nucleoside di- and monophosphates and free phosphate. The divalent cation requirement for this activity of e sigma A was further examined by the addition of Mn(2+), Mg(2+), Ca(2+), and Zn(2+) ions. NTP hydrolysis by e sigma A was maximal when Mn(2+), Mg(2+), or Ca(2+) concentrations were 5, 4, or 1 mM, respectively. Addition of Mn(2+) or Mg(2+) stimulated the reactions up to 4- or 3-fold, respectively, higher than Ca(2+) (2.2-fold). However, Zn(2+) ion inhibited this activity of e sigma A. The results suggest that nucleotidyl phosphatase activity of e sigma A is absolutely dependent on the divalent cations Mn(2+), Mg(2+), or Ca(2+), but not Zn(2+). Similar results were obtained from the analysis of divalent cation requirements for the protein sigma A nucleotidyl phosphatase activity. Optimal pH for nucleotidyl phosphatase activity of protein sigma A from both preparations was determined using reaction mixtures buffered at different pH. The results show that the optimal activities of both proteins were similar and were achieved between pH 7.5 and 8.5.
Authors:
Hsien Sheng Yin; Yu Pin Su; Long Huw Lee
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Virology     Volume:  293     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-03-11     Completed Date:  2002-05-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  United States    
Other Details:
Languages:  eng     Pagination:  379-85     Citation Subset:  IM    
Affiliation:
Department of Veterinary Medicine, National Chung Hsing University, Taichung 403, Taiwan.
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MeSH Terms
Descriptor/Qualifier:
Acid Anhydride Hydrolases / genetics,  metabolism*
Animals
Calcium / pharmacology
Cations, Divalent
Cells, Cultured
Chickens
Dose-Response Relationship, Drug
Escherichia coli / genetics
Hydrogen-Ion Concentration
Hydrolysis / drug effects
Magnesium / pharmacology
Manganese / pharmacology
Nucleoside-Triphosphatase
Orthoreovirus, Avian / metabolism*
Recombinant Proteins / metabolism
Viral Core Proteins / isolation & purification,  metabolism*
Zinc / pharmacology
Chemical
Reg. No./Substance:
0/Cations, Divalent; 0/Recombinant Proteins; 0/Viral Core Proteins; 7439-95-4/Magnesium; 7439-96-5/Manganese; 7440-66-6/Zinc; 7440-70-2/Calcium; 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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