Differential Expression, Tissue-Specific Distribution, and Posttranslational Controls of Phosphoenolpyruvate Carboxylase

• Published in: Plants (Basel) Vol. 10; no. 9; p. 1887
• Main Authors: Caburatan, Lorrenne, Park, Joonho
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 13-09-2021; MDPI
• Subjects: Carbon dioxide; Carbon dioxide fixation; Chloroplasts; Crassulacean acid metabolism; Developmental stages; differential expression; Environmental effects; Enzymes; Flowers; Gene expression; Leaves; Localization; Malate; Metabolism; Organs; Phosphoenolpyruvate carboxylase; Phosphorylation; Photosynthesis; Plants; Polypeptides; posttranslational modification; Review; Seeds; single-cell C4 plant; Sorghum; tissue-specific expression; Ubiquitination; single-cell C4 plant; posttranslational modification; phosphoenolpyruvate carboxylase; differential expression; tissue-specific expression; monoubiquitination; phosphorylation
• ISSN: 2223-7747; 2223-7747
• DOI: 10.3390/plants10091887

Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme, which is crucial for plant carbon metabolism. PEPC participates in photosynthesis by catalyzing the initial fixation of atmospheric CO
and is abundant in both C
and crassulacean acid metabolism leaves. PEPC is differentially expressed at different stages of plant development, mostly in leaves, but also in developing seeds. PEPC is known to show tissue-specific distribution in leaves and in other plant organs, such as roots, stems, and flowers. Plant PEPC undergoes reversible phosphorylation and monoubiquitination, which are posttranslational modifications playing important roles in regulatory processes and in protein localization. Phosphorylation activates the PEPC enzyme, making it more sensitive to glucose-6-phosphate and less sensitive to malate or aspartate. PEPC phosphorylation is known to be diurnally regulated and delicately changed in response to various environmental stimuli, in addition to light. PEPCs belong to a small gene family encoding several plant-type and distantly related bacterial-type PEPCs. This paper provides a minireview of the general information on PEPCs in both C
and C
plants.