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Titolo:
IN-VIVO AND IN-VITRO PHOSPHORYLATION OF THE PHOSPHOENOLPYRUVATE CARBOXYLASE FROM WHEAT SEEDS DURING GERMINATION
Autore:
OSUNA L; GONZALEZ MC; CEJUDO FJ; VIDAL J; ECHEVARRIA C;
Indirizzi:
UNIV SEVILLE,FAC BIOL,DEPT BIOL VEGETAL,AVE REINA MERCEDES 6 E-41012 SEVILLE SPAIN UNIV SEVILLE,FAC BIOL,DEPT BIOL VEGETAL E-41012 SEVILLE SPAIN UNIV SEVILLA,CSIC,FAC QUIM,INST BIOQUIM VEGETAL & FOTOSINTESIS E-41080 SEVILLE SPAIN UNIV PARIS 11,CTR ORSAY,CNRS,URA D1128,INST BIOTECHNOL PLANTES ORSAY FRANCE
Titolo Testata:
Plant physiology
fascicolo: 2, volume: 111, anno: 1996,
pagine: 551 - 558
SICI:
0032-0889(1996)111:2<551:IAIPOT>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-SERINE KINASE; LIGHT DARK REGULATION; INVIVO PHOSPHORYLATION; SORGHUM; MAIZE; ENDOSPERM; PHOTOSYNTHESIS; ACIDIFICATION; SEQUENCE; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
L. Osuna et al., "IN-VIVO AND IN-VITRO PHOSPHORYLATION OF THE PHOSPHOENOLPYRUVATE CARBOXYLASE FROM WHEAT SEEDS DURING GERMINATION", Plant physiology, 111(2), 1996, pp. 551-558

Abstract

Phosphoenolpyruvate carboxylase (PEPC) activity was detected in the aleurone endosperm of wheat (Triticum aestivum cv Chinese Spring) seeds, and specific anti-Sorghum C-4 PEPC polyclonal antibodies cross-reacted with 103- and 100-kD polypeptides present in dry seeds and seeds that had imbibed; in addition, a new, 108-kD polypeptide was detected 6 h after imbibition. The use of specific anti-phosphorylation-site immunoglobulin G (APS-IgG) identified the presence of a phosphorylation motif equivalent to that round in other plant PEPCs studied so Tar. The binding of this APS-IgG to the target protein promoted changes in the properties of seed PEPC similar to those produced by phosphorylation, as previously shown for the recombinant Sorghum leaf C-4 PEPC. In desalted seed extracts, an endogenous PEPC kinase activity catalyzed a bona fide phosphorylation of the target protein, as deduced from the immunoinhibition of the in vitro phosphorylation reaction by the APS-IgG. In addition, the major, 103-kD PEPC polypeptide was also shown to be radiolabeled in situ 48 h after imbibition in [P-32]orthophosphate. Theratio between optimal (pH 8) and suboptimal (pH 7.3 or 7.1) PEPC activity decreased during germination, thereby suggesting a change in catalytic rate related to an in vivo phosphorylation process. These collective data document that the components needed for the regulatory phosphorylation of PEPC are present and functional during germination of wheat seeds.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 01:27:42