Further analysis of cDNA clones for maize phospho<i>enol</i>pyruvate carboxylase involved in C<sub>4</sub> photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo

Yanagisawa, Shuichi; Izui, Katsura; Yamaguchi, Yasunori; Shigesada, Katsuya; Katsuki, Hirohiko

doi:10.1016/0014-5793(88)80807-x

Cited by 51 publications

(10 citation statements)

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“…pTM94 and pEM94 (27), which contain the entire coding region of the cDNA of ZmPEPC, were used as starting materials. During the course of this study, many errors were found in the sequence that had been reported by us previously (28,29). Thus we re-determined and revised the sequence (Fig.…”

Section: Methodsmentioning

confidence: 79%

Maize Phosphoenolpyruvate Carboxylase

Takahashi-Terada

Kotera

Ohshima

et al. 2005

Journal of Biological Chemistry

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Phosphoenolpyruvate carboxylases (PEPC, EC 4.1.1.31) from higher plants are regulated by both allosteric effects and reversible phosphorylation. Previous x-ray crystallographic analysis of Zea mays PEPC has revealed a binding site for sulfate ion, speculated to be the site for an allosteric activator, glucose 6-phosphate (Glc-6-P) (Matsumura, H., Xie, Y., Shirakata, S., Inoue, T., Yoshinaga, T., Ueno, Y., Izui, K., and Kai, Y. (2002) Structure (Lond.) 10, 1721-1730). Because kinetic experiments have also supported this notion, each of the four basic residues (Arg-183, -184, -231, and -372 on the adjacent subunit) located at or near the binding site was replaced by Gln, and the kinetic properties of recombinant mutant enzymes were investigated. Complete desensitization to Glc-6-P was observed for R183Q, R184Q, R183Q/R184Q (double mutant), and R372Q, as was a marked decrease in the sensitivity for R231Q. The heterotropic effect of Glc-6-P on an allosteric inhibitor, L-malate, was also abolished, but sensitivity to Gly, another allosteric activator of monocot PEPC, was essentially not affected, suggesting the distinctness of their binding sites. Considering the kinetic and structural data, Arg-183 and Arg-231 were suggested to be involved directly in the binding with phosphate group of Glc-6-P, and the residues Arg-184 and Arg-372 were thought to be involved in making up the site for Glc-6-P and/or in the transmission of an allosteric regulatory signal. Most unexpectedly, the mutant enzymes had almost lost responsiveness to regulatory phosphorylation at Ser-15. An apparent lack of kinetic competition between the phosphate groups of Glc-6-P and of phospho-Ser at 15 suggested the distinctness of their binding sites. The possible roles of these Arg residues are discussed.

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Section: Methodsmentioning

confidence: 79%

Maize Phosphoenolpyruvate Carboxylase

Takahashi-Terada

Kotera

Ohshima

et al. 2005

Journal of Biological Chemistry

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“…Consensus intron/exon splice sites (aGGTaag-tgcAGg) are conserved. Generally, a classical gene organization is observed, although in some C 4 -and C 3 -type Ppc genes there is no typical TATA box, and multiple polyadenylation sites are found in the 3′-untranslated region (15,43,74,132).…”

Section: Ppc and Pepc Sequence Comparisonsmentioning

confidence: 99%

PHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants

Chollet

Vidal

O’Leary³

1996

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

644

559

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Since plant phosphoenolpyruvate carboxylase (PEPC) was last reviewed in the Annual Review of Plant Physiology over a decade ago (O'Leary 1982), significant advances have been made in our knowledge of this oligomeric, cytosolic enzyme. This review highlights this exciting progress in plant PEPC research by focusing on the three major areas of recent investigation: the enzymology of the protein; its posttranslational regulation by reversible protein phosphorylation and opposing metabolite effectors; and the structure, expression, and molecular evolution of the nuclear PEPC genes. It is hoped that the next ten years will be equally enlightening, especially with respect to the three-dimensional structure of the plant enzyme, the molecular analysis of its highly regulated protein-Ser/ Thr kinase, and the elucidation of its associated signal-transduction pathways in various plant cell types.

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“…In vitro phosphorylation of PEPC by an endogenous protein kinase and accompanying changes in the kinetic properties were also reported [4]. Although the complete primary structure of maize PEPC involved in the C4 photosynthesis was deduced from the nucleotide sequence of the cDNA by us [5,6], the site of the seryl residue which undergoes phosphorylation has not yet been elucidated. In this study, we found that the maize PEPC was a good substrate for mammalian A-kinase in vitro and that the phosphorylation caused the changes in kinetic properties, which were very similar to the phosphorylation observed in vivo [3].…”

Section: Introductionmentioning

confidence: 98%

Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser¹⁵ with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate

et al. 1990

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The so‐called light‐activation of phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.31) involved in C4 photosynthesis is known to be mediated by phosphorylation. A cyclic AMP‐dependent protein kinase from bovine heart was found to be able to phosphorylate PEPC. The phosphorylation was accompanied by the changes in kinetic properties, which were very similar to the reported light activation. The phosphorylated amino acid residue was identified as Ser and the position of this Ser on the primary structure [(1988) FEBS Lett. 229, 107‐110] was determined to be Ser15.

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Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C₄ photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo

Cited by 51 publications

References 17 publications

Maize Phosphoenolpyruvate Carboxylase

Maize Phosphoenolpyruvate Carboxylase

PHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants

Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser¹⁵ with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate

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Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo

Cited by 51 publications

References 17 publications

Maize Phosphoenolpyruvate Carboxylase

Maize Phosphoenolpyruvate Carboxylase

PHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants

Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate

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Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C₄ photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo

Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser¹⁵ with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate