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C2 domain is responsible for targeting rice phosphoinositide specific phospholipase C

Rupwate, Sunny D and Rajasekharan, Ram (2012) C2 domain is responsible for targeting rice phosphoinositide specific phospholipase C. In: Plant Molecular Biology, 78 (3). pp. 247-258.

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Official URL: http://www.springerlink.com/content/u10v8187t87688...

Abstract

Phosphoinositide-specific phospholipase C (PLC) is involved in Ca2+ mediated signalling events that lead to altered cellular status. Using various sequence-analysis methods, we identified two conserved motifs in known PLC sequences. The identified motifs are located in the C2 domain of plant PLCs and are not found in any other protein. These motifs are specifically found in the Ca2+ binding loops and form adjoining beta strands. Further, we identified certain conserved residues that are highly distinct from corresponding residues of animal PLCs. The motifs reported here could be used to annotate plant-specific phospholipase C sequences. Furthermore, we demonstrated that the C2 domain alone is capable of targeting PLC to the membrane in response to a Ca2+ signal. We also showed that the binding event results from a change in the hydrophobicity of the C2 domain upon Ca2+ binding. Bioinformatic analyses revealed that all PLCs from Arabidopsis and rice lack a transmembrane domain, myristoylation and GPI-anchor protein modifications. Our bioinformatic study indicates that plant PLCs are located in the cytoplasm, the nucleus and the mitochondria. Our results suggest that there are no distinct isoforms of plant PLCs, as have been proposed to exist in the soluble and membrane associated fractions. The same isoform could potentially be present in both subcellular fractions, depending on the calcium level of the cytosol. Overall, these data suggest that the C2 domain of PLC plays a vital role in calcium signalling.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Springer.
Keywords: Plant phosphoplipase C;C2 domain;Membrane targeting;Surface hydrophobicity;Phospholipids
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 18 May 2012 07:52
Last Modified: 18 May 2012 07:56
URI: http://eprints.iisc.ernet.in/id/eprint/44407

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