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PPC3  -  phosphoenolpyruvate carboxylase 3

Arabidopsis thaliana

Synonyms: ATPPC3
 
 
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Disease relevance of ATPPC3

  • Here, we describe a gene from Arabidopsis, stated as Atppc4, encoding a PEPC, which shows more similarity to Escherichia coli than to plant PEPCs [1].
  • The phylogenetic analysis suggests that both plant-type and bacterial-type PEPCs diverged early during the evolution of plants from a common ancestor, probably the PEPC from gamma-proteobacteria [1].
  • Among them, the calcium-dependent protein kinase and phosphoenolpyruvate carboxylase kinase families are specific for plants, whereas the Ca(2+)/calmodulin-dependent protein kinase and provirus insertion in mouse-like kinase families were found only in yeast and animals [2].
 

High impact information on ATPPC3

  • Coenzyme A biosynthesis in plants is not fully understood, and to date only the AtHAL3a (AtCoaC) gene of Arabidopsis thaliana has been cloned and identified as 4'-phosphopantothenoylcysteine (PPC) decarboxylase (Kupke, T., Hernández-Acosta, P., Steinbacher, S., and Culiáñez-Macià, F. A. (2001) J. Biol. Chem. 276, 19190-19196) [3].
  • We report the expression patterns of five PEPC genes, including one encoding a bacterial-type PEPc lacking the phosphorylation site of the plant-type PEPcs [4].
  • We have analyzed the expression of both PPCK genes and the PEPC genes that encode PEPc in soybean (Glycine max) [4].
  • Hypo-osmotic treatment of the cells increased the amount of PEPC that bound the PA beads without increasing the absolute amount of PEPC [5].
  • As most plant PEPC genes, Atppc1, Atppc2, and Atppc3 are formed by 10 exons interrupted by nine introns [1].
 

Biological context of ATPPC3

  • Interestingly, this enzyme lacks the phosphorylation domain, hence indicating that it is a bacterial-type PEPC [1].
  • Salt and drought exerted a differential induction of PEPC gene expression in roots, Atppc4 showing the highest induction in response to both stresses [6].
  • AHL1 contains an AT-hook motif and unknown conserved PPC (plants and prokaryotes conserved) domain that includes a hydrophobic region [7].
  • The AT-hook motif was essential for matrix attachment region (MAR) binding, and the hydrophobic region of the PPC was indispensable for nuclear localization [7].
  • Our results suggest that AHL1 is a novel plant MAR binding protein, which is related to the positioning of chromatin fibers in the nucleus by the presence of an AT-hook motif and PPC domain [7].
 

Analytical, diagnostic and therapeutic context of ATPPC3

  • Based on sequence analysis it was deduced that Atppc1, Atppc2 and Atppc3 genes encode plant-type PEPCs, whereas Atppc4 encodes a PEPC without phosphorylation motif, but no data at the protein level have been reported [6].
  • Western-blot analysis of different Arabidopsis organs probed with anti plant-type PEPC antibodies detected a double band, the one with low molecular weight corresponding to the three plant-type PEPCs [6].

References

  1. Identification and expression analysis of a gene encoding a bacterial-type phosphoenolpyruvate carboxylase from Arabidopsis and rice. Sánchez, R., Cejudo, F.J. Plant Physiol. (2003) [Pubmed]
  2. Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae. Wang, D., Harper, J.F., Gribskov, M. Plant Physiol. (2003) [Pubmed]
  3. 4'-phosphopantetheine and coenzyme A biosynthesis in plants. Kupke, T., Hernández-Acosta, P., Culiáñez-Macià, F.A. J. Biol. Chem. (2003) [Pubmed]
  4. Roots, cycles and leaves. Expression of the phosphoenolpyruvate carboxylase kinase gene family in soybean. Sullivan, S., Jenkins, G.I., Nimmo, H.G. Plant Physiol. (2004) [Pubmed]
  5. Isolation and identification of phosphatidic acid targets from plants. Testerink, C., Dekker, H.L., Lim, Z.Y., Johns, M.K., Holmes, A.B., Koster, C.G., Ktistakis, N.T., Munnik, T. Plant J. (2004) [Pubmed]
  6. Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress. Sánchez, R., Flores, A., Cejudo, F.J. Planta (2006) [Pubmed]
  7. Identification of a novel plant MAR DNA binding protein localized on chromosomal surfaces. Fujimoto, S., Matsunaga, S., Yonemura, M., Uchiyama, S., Azuma, T., Fukui, K. Plant Mol. Biol. (2004) [Pubmed]
 
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