Document Detail


Molecular cloning and characterization of a soluble inorganic pyrophosphatase in potato.
MedLine Citation:
PMID:  8552717     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A cDNA clone encoding a soluble inorganic pyrophosphatase (EC 3.6.1.1) of potato (Solanum tuberosum L.) was isolated by screening a developing tuber library with a heterologous probe. The central domain of the encoded polypeptide is nearly identical at the sequence level with its Arabidopsis homolog (J.J. Kieber and E.R. Signer [1991] Plant Mol Biol 16: 345-348). Computer-assisted analysis of the potato, Arabidopsis, and Escherichia coli soluble pyrophosphatases indicated a remarkably conserved organization of the hydrophobic protein domains. The enzymatic function of the potato protein could be deduced from the presence of amino acid residues highly conserved in soluble pyrophosphatases and was confirmed by its capacity to complement a thermosensitive pyrophosphatase mutation in E. coli. The potato polypeptide was purified from complemented bacterial cells and its pyrophosphatase activity was shown to be strictly dependent on Mg2+ and strongly inhibited by Ca2+. The subcellular location of the potato pyrophosphatase is unknown. Structure analysis of the N-terminal protein domain failed to recognize typical transit peptides and the calculated molecular mass of the polypeptide (24 kD) is significantly inferior to the values reported for the plastidic (alkaline) or mitochondrial pyrophosphatases in plants (28-42 kD). Two unlinked loci could be mapped by restriction fragment length polymorphism analysis in the potato genome using the full-length cDNA as probe.
Authors:
P du Jardin; J Rojas-Beltran; C Gebhardt; R Brasseur
Related Documents :
23255617 - Early secretory pathway localization and lack of processing for hepatitis e virus repli...
12221287 - Folate synthesis in plants: the first step of the pterin branch is mediated by a unique...
23345897 - Targeted green-red photoconversion of eosfp, a fluorescent marker protein.
10432637 - A bean cdna expressed during a hypersensitive reaction encodes a putative calcium-bindi...
2647737 - The flexible region of protein l12 from bacterial ribosomes studied by proton nuclear m...
14654357 - Improved diagnostic testing for ataxia-telangiectasia by immunoblotting of nuclear lysa...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Plant physiology     Volume:  109     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  1995 Nov 
Date Detail:
Created Date:  1996-02-22     Completed Date:  1996-02-22     Revised Date:  2010-09-13    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  853-60     Citation Subset:  IM    
Affiliation:
Department of Plant Biology, Faculty of Agricultural Sciences of Gembloux, Belgium.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/Z36894
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Base Sequence
Chromosome Mapping
DNA, Complementary / genetics
Escherichia coli / genetics
Gene Library
Genes, Plant
Genetic Complementation Test
Inorganic Pyrophosphatase
Magnesium / pharmacology
Molecular Sequence Data
Multigene Family
Polymorphism, Restriction Fragment Length
Pyrophosphatases / biosynthesis,  drug effects,  genetics*
Recombinant Proteins / biosynthesis
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Solanum tuberosum / enzymology,  genetics*
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/Recombinant Proteins; 7439-95-4/Magnesium; EC 3.6.1.-/Pyrophosphatases; EC 3.6.1.1/Inorganic Pyrophosphatase
Comments/Corrections

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


Previous Document:  A structural model for the mechanisms of elicitor release from fungal cell walls by plant beta-1,3-e...
Next Document:  Copper-sensitive mutant of Arabidopsis thaliana.