Document Detail


Characterization of the AGPase large subunit isoforms from tomato indicates that the recombinant L3 subunit is active as a monomer.
MedLine Citation:
PMID:  20236089     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The enzyme AGPase [ADP-Glc (glucose) pyrophosphorylase] catalyses a rate-limiting step in starch synthesis in tomato (Solanum lycopersicon) fruit, which undergoes a transient period of starch accumulation. It has been a generally accepted paradigm in starch metabolism that the enzyme naturally functions primarily as a heterotetramer comprised of two large subunits (L) and two small subunits (S). The tomato genome harbours a single gene encoding S and three genes for L proteins, which are expressed in both a tissue- and time-specific manner. In the present study the allosteric contributions of the different L subunits were compared by expressing each one in Escherichia coli, in conjunction with S and individually, and characterizing the resulting enzyme activity. Our results indicate different kinetic characteristics of the tomato L1/S and L3/S heterotetramers. Surprisingly, the recombinant L3 protein was also active when expressed alone and size-exclusion and immunoblotting showed that it functioned as a monomer. Subunit interaction modelling pointed to two amino acids potentially affecting subunit interactions. However, directed mutations did not have an impact on subunit tetramerization. These results indicate a hitherto unknown active role for the L subunit in the synthesis of ADP-Glc.
Authors:
Marina Petreikov; Miriam Eisenstein; Yelena Yeselson; Jack Preiss; Arthur A Schaffer
Related Documents :
18540679 - The stoichiometry of subunit c of escherichia coli atp synthase is independent of its r...
10617639 - Serine acetyltransferase from escherichia coli is a dimer of trimers.
8126719 - Asymmetric arrangement of two alpha subunits within escherichia coli rna polymerase. in...
19672299 - Subcomplex ilambda specifically controls integrated mitochondrial functions in caenorha...
454619 - Functional identity of catalytic subunits of acetylcholinesterase.
11279119 - Adjacent basic amino acid residues recognized by the cop i complex and ubiquitination g...
19374909 - Crystal structure of red chlorophyll catabolite reductase: enlargement of the ferredoxi...
8013449 - Three-dimensional structure of endo-1,4-beta-xylanase ii from trichoderma reesei: two c...
20864339 - Antidotes to anthrax lethal factor intoxication. part 1: discovery of potent lethal fac...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-05-13
Journal Detail:
Title:  The Biochemical journal     Volume:  428     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-13     Completed Date:  2010-05-25     Revised Date:  2010-09-22    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  201-12     Citation Subset:  IM    
Affiliation:
Department of Vegetable Research, Volcani Center-ARO, Bet Dagan 50250, Israel.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Blotting, Western
Escherichia coli / genetics,  metabolism
Glucose-1-Phosphate Adenylyltransferase / chemistry,  genetics,  metabolism*
Kinetics
Lycopersicon esculentum / enzymology*,  genetics
Mutagenesis, Site-Directed
Plant Proteins / chemistry,  genetics,  metabolism*
Protein Isoforms / chemistry,  genetics,  metabolism*
Protein Subunits / chemistry,  genetics,  metabolism*
Recombinant Proteins / chemistry,  genetics,  metabolism*
Tandem Mass Spectrometry
Chemical
Reg. No./Substance:
0/Plant Proteins; 0/Protein Isoforms; 0/Protein Subunits; 0/Recombinant Proteins; EC 2.7.7.27/Glucose-1-Phosphate Adenylyltransferase

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


Previous Document:  The patented uses of D-ribose in cardiovascular diseases.
Next Document:  C-terminal domain phosphorylation of ERK3 controlled by Cdk1 and Cdc14 regulates its stability in mi...