Idioma:

Light activation of maize phosphoenolpyruvate carboxylase protein-serine kinase activity is inhibited by mesophyll and bundle sheath-directed photosynthesis inhibitors

Jiao, J.A. (University of California, Berkeley, CA) ; Chollet, R

Plant physiology (Bethesda), 1992-01, Vol.98 (1), p.152-156 [Periódico revisado por pares]

ROCKVILLE: AMER SOC PLANT PHYSIOLOGISTS

Texto completo disponível

Citações Citado por

Enviar para

Título:
Light activation of maize phosphoenolpyruvate carboxylase protein-serine kinase activity is inhibited by mesophyll and bundle sheath-directed photosynthesis inhibitors
Autor: Jiao, J.A. (University of California, Berkeley, CA) ; Chollet, R
Assuntos: ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Biological and medical sciences ; FOSFENOLPIRUVATO CARBOXILASA ; FOTOSINTESIS ; Fundamental and applied biological sciences. Psychology ; INHIBICION ; INHIBITION ; Life Sciences & Biomedicine ; LUMIERE ; LUZ ; MESOFILO ; MESOPHYLLE ; Metabolism ; PHOSPHOENOLPYRUVATE CARBOXYLASE ; PHOTOSYNTHESE ; Photosynthesis, respiration. Anabolism, catabolism ; Plant physiology and development ; Plant Sciences ; PROTEINA QUINASA ; PROTEINE KINASE ; Science & Technology ; ZEA MAYS
É parte de: Plant physiology (Bethesda), 1992-01, Vol.98 (1), p.152-156
Notas: F60
9180784
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: C4 phosphoenolpyruvate carboxylase (PEPC) is post-translationally regulated by reversible phosphorylation of a specific N-terminal seryl residue in response to light/dark transitions of the parent leaf tissue. The protein-serine kinase (PEPC-PK) that phosphorylates/activates this mesophyll-cytoplasm target enzyme is slowly, but strikingly, activated by high light and inactivated in darkness in vivo by a mechanism involving cytoplasmic protein synthesis/degradation as a primary component. In this report, evidence is presented indicating that the inhibition of Calvin cycle activity by a variety of mesophyll (3-(3,4-dichloro-phenyl)-1,1-dimethylurea, isocil, methyl viologen) and bundle sheath (DL-glyceraldehyde)-directed photosynthesis inhibitors blocks the light activation of maize (Zea mays L.) PEPC-PK and the ensuing regulatory phosphorylation of its target enzyme in vivo. Based on these and related observations, we propose that the Calvin cycle supplies the C4 mesophyll cell with (a) a putative signal (e.g. phosphorylated metabolite, amino acid) that interacts with the cytoplasmic protein synthesis event to effect the light activation of PEPC-PK and the concomitant phosphorylation of PEPC, and (b) high levels of known positive effectors (e.g. triosephosphate, glucose-6-phosphate) that interact directly with the carboxylase. The combined result of this complex regulatory cascade is to effectively desensitize PEPC to feedback inhibition by the millimolar levels of L-malate required for rapid diffusive transport to the bundle sheath during high rates of C4 photosynthesis
Editor: ROCKVILLE: AMER SOC PLANT PHYSIOLOGISTS
Idioma: Inglês

Links

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Light activation of maize phosphoenolpyruvate carboxylase protein-serine kinase activity is inhibited by mesophyll and bundle sheath-directed photosynthesis inhibitors

Jiao, J.A. (University of California, Berkeley, CA) ; Chollet, R

ROCKVILLE: AMER SOC PLANT PHYSIOLOGISTS

Buscando em bases de dados remotas. Favor aguardar.