INVESTIGADORES
IGLESIAS Alberto Alvaro
artículos
Título:
Molecular Cloning and Expression of the Gene Encoding ADPglucose Pyrophosphorylase from Cyanobacterium Anabaena sp. Strain PCC 7120
Autor/es:
Y.-Y. CHARNG, G. KAKEFUDA, A.A. IGLESIAS, W.J. BUIKEMA Y J. PREISS
Revista:
PLANT MOLECULAR BIOLOGY
Referencias:
Año: 1992 vol. 20 p. 37 - 47
ISSN:
0167-4412
Resumen:
Plant Mol Biol. 1992 Oct;20(1):37-47.
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-->LinksMolecular
cloning and expression of the gene encoding ADP-glucose
pyrophosphorylase from the cyanobacterium Anabaena sp. strain PCC 7120.Charng YY, Kakefuda G, Iglesias AA, Buikema WJ, Preiss J.Dept. of Biochemistry, Michigan State University, East Lansing 48824.Previous
studies have indicated that ADP-glucose pyrophosphorylase (ADPGlc
PPase) from the cyanobacterium Anabaena sp. strain PCC 7120 is more
similar to higher-plant than to enteric bacterial enzymes in
antigenicity and allosteric properties. In this paper, we report the
isolation of the Anabaena ADPGlc PPase gene and its expression in
Escherichia coli. The gene we isolated from a genomic library utilizes
GTG as the start codon and codes for a protein of 48,347 Da which is in
agreement with the molecular mass determined by SDS-PAGE for the
Anabaena enzyme. The deduced amino acid sequence is 63, 54, and 33%
identical to the rice endosperm small subunit, maize endosperm large
subunit, and the E. coli sequences, respectively. Southern analysis
indicated that there is only one copy of this gene in the Anabaena
genome. The cloned gene encodes an active ADPGlc PPase when expressed
in an E. coli mutant strain AC70R1-504 which lacks endogenous activity
of the enzyme. The recombinant enzyme is activated and inhibited
primarily by 3-phosphoglycerate and Pi, respectively, as is the native
Anabaena ADPGlc PPase. Immunological and other biochemical studies
further confirmed the recombinant enzyme to be the Anabaena enzyme.