Protein turnover as a component in the light/dark regulation of phosphoenolpyruvate carboxylase protein-serine kinase activity in C4 plants.

Jiao, Jin-an; Echevarrı́a, Cristina; Vidal, Jean; Chollet, Raymond

doi:10.1073/pnas.88.7.2712

Cited by 84 publications

(89 citation statements)

References 26 publications

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“…However, it must be emphasized that the detached tobacco leaves became severely wilted soon after application of 5 JLIM CHX. This overt symptom of severe water loss was previously observed neither with leaves excised from maize (Jiao et al, 1991a), sorghum (Bakrim et al, 1993), wheat (Bakrim et al, 1993;, and spinach (Weiner et al, 1992) plants nor with any of the other inhibitor treatments used in the present study.…”

Section: Light Activation Of Tobacco Leaf Pepc-kinase Is Reversible Amentioning

confidence: 78%

“…In the former, light activates and darkness inactivates the kinase in vivo (Echevarria et al, 1990;Jiao and Chollet, 1991;Nimmo, 1993). Moreover, treatment of C, leaves with inhibitors of photosynthesis or cytosolic protein synthesis prevents this light activation of PEPC-PK (Jiao et al, 1991a;Bakrim et al, 1992Bakrim et al, , 1993Jiao and Chollet, 1992;Li and Chollet, 1993), implicating the involvement of photosynthesis and protein turnover in the light-signal transduction pathway. Cytosolic levels of Ca2+, pH, and certain photosynthetic metabolites also have been suggested as signaling elements in the light activation of C, PEPC-PK in situ Duff et al, 1996;Giglioli-Guivarc'h et al, 1996).…”

mentioning

confidence: 99%

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Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Zhang

Chollet

1996

Plant Physiology

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We have previously reported the partial purification of a Ca2+- independent phosphoenolpyruvate carboxylase (PEPC) protein-serine/threonine kinase (PEPC-PK) from illuminated leaves of N-sufficient tobacco (Nicotiana tabacum L.) plants (Y.-H. Wang, R. Chollet [1993] FEBS Lett 328: 215–218). We now report that this C3 PEPC-kinase is reversibly light activated in vivo in a time-dependent manner. As the kinase becomes light activated, the activity and L-malate sensitivity of its target protein increases and decreases, respectively. The light activation of tobacco PEPC-PK is prevented by pretreatment of detached leaves with various photosynthesis and cytosolic protein-synthesis inhibitors. Similarly, specific inhibitors of glutamine synthetase block the light activation of tobacco leaf PEPC-kinase under both photorespiratory and nonphotorespiratory conditions. This striking effect is partially and specifically reversed by exogenous glutamine, whereas it has no apparent effect on the light activation of the maize (Zea mays L.) leaf kinase. Using an in situ “activity-gel” phosphorylation assay, we have identified two major Ca2+-independent PEPC-kinase catalytic polypeptides in illuminated tobacco leaves that have the same molecular masses (approximately 30 and 37 kD) as found in illuminated maize leaves. Collectively, these results indicate that the phosphorylation of PEPC in N-sufficient leaves of tobacco (C3) and maize (C4) is regulated through similar but not identical light-signal transduction pathways.

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Section: Light Activation Of Tobacco Leaf Pepc-kinase Is Reversible Amentioning

confidence: 78%

mentioning

confidence: 99%

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Zhang

Chollet

1996

Plant Physiology

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“…For half-seed experiments, dry, ungerminated rice seeds were sliced with a razor blade into embryo-containing and embryoless halves, incubated separately in petri dishes on moist paper towels in the dark, and wet daily with either distilled water or 5 μM cycloheximide (Jiao et al 1991).…”

Section: Plant Growthmentioning

confidence: 99%

Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types

et al. 2001

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Shearman, L.; Mathiesen, M.; Zhou, Y.J.; Arredondo-Peter, R.; Sarath, Gautam; and Klucas, R. V., "Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types" (2001 Abstract: Nonsymbiotic hemoglobins (ns-Hbs) previously have been found in monocots and dicots; however, very little is known about the tissue and cell type localization as well as the physiological function(s) of these oxygen-binding proteins. We report the immunodetection and immunolocalization of ns-Hbs in rice (Oryza sativa L.) by Western blotting and in situ confocal laser scanning techniques. Ns-Hbs were detected in soluble extracts of different tissues from the developing rice seedling by immunoblotting. Levels of ns-Hbs increased in the germinating seed for the fi rst six days following imbibition and remained relatively constant thereafter. In contrast, ns-Hb levels decreased during leaf maturation. Roots and mesocotyls contained detectable, but low levels of ns-Hbs. Split-seed experiments revealed that ns-Hbs are synthesized de novo during seed germination and are expressed in the absence of any signal originating from the embryo. Immunolocalization of ns-Hbs by con-focal microscopy indicated the presence of ns-Hbs primarily in differentiated and differentiating cell types of the developing seedling, such as the aleurone, scutellum, root cap cells, sclerenchyma, and tracheary elements. To our knowledge, this is the fi rst report of the specifi c cellular localization of these proteins during seedling development.

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“…Phosphorylation of PEPCase desensitizes the enzyme to feedback inhibition by malate and serves to activate the enzyme during times of active fixation of CO 2 into oxaloacetic acid. PPCK activity appears to be regulated at the level of transcription and is under the control of light in C 4 plants and a circadian rhythm in crassulacean acid metabolism plants (Jiao et al, 1991;Vidal and Chollet, 1997;Hartwell et al, 1999aHartwell et al, , 1999bNimmo, 2000).…”

Section: Ppck and Peprkmentioning

confidence: 99%

The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

Hrabak

Chan²,

Gribskov³

et al. 2003

Plant Physiology

898

823

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The CDPK-SnRK superfamily consists of seven types of serine-threonine protein kinases: calcium-dependent protein kinase (CDPKs), CDPK-related kinases (CRKs), phosphoenolpyruvate carboxylase kinases (PPCKs), PEP carboxylase kinase-related kinases (PEPRKs), calmodulin-dependent protein kinases (CaMKs), calcium and calmodulin-dependent protein kinases (CCaMKs), and SnRKs. Within this superfamily, individual isoforms and subfamilies contain distinct regulatory domains, subcellular targeting information, and substrate specificities. Our analysis of the Arabidopsis genome identified 34 CDPKs, eight CRKs, two PPCKs, two PEPRKs, and 38 SnRKs. No definitive examples were found for a CCaMK similar to those previously identified in lily (Lilium longiflorum) and tobacco (Nicotiana tabacum) or for a CaMK similar to those in animals or yeast. CDPKs are present in plants and a specific subgroup of protists, but CRKs, PPCKs, PEPRKs, and two of the SnRK subgroups have been found only in plants. CDPKs and at least one SnRK have been implicated in decoding calcium signals in Arabidopsis. Analysis of intron placements supports the hypothesis that CDPKs, CRKs, PPCKs and PEPRKs have a common evolutionary origin; however there are no conserved intron positions between these kinases and the SnRK subgroup. CDPKs and SnRKs are found on all five Arabidopsis chromosomes. The presence of closely related kinases in regions of the genome known to have arisen by genome duplication indicates that these kinases probably arose by divergence from common ancestors. The PlantsP database provides a resource of continuously updated information on protein kinases from Arabidopsis and other plants.In eukaryotes, protein kinases are involved in regulating key aspects of cellular function, including cell division, metabolism, and responses to external signals. The completed sequence of the Arabidopsis genome provides the first opportunity to identify all of the protein kinases present in a model plant. The Arabidopsis genome encodes 1,085 typical protein kinases (M. Gribskov, unpublished data), which is about 4% of the predicted 25,500 genes (Arabidopsis Article, publication date, and citation information can be found at www.plantphysiol.org/cgi

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Protein turnover as a component in the light/dark regulation of phosphoenolpyruvate carboxylase protein-serine kinase activity in C4 plants.

Cited by 84 publications

References 26 publications

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types

The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases

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