Bioinformatics

Protein phosphorylation/dephosphorylation through protein kinases is a key regulatory mechanism in modulating the activation of intracellular responses to extracellular information. The mitogen-activated protein kinase (MAPK) cascades are known to be one of the

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major phosphorylation pathways which function downstream of sensors/receptors and regulate cellularresponses to external and endogenous stimuli.

Mitogen activated protein kinase (MAPK) cascades are universal signal transduction modules that play crucial role in plant growth and development as well as biotic and abiotic stress responses. 20 and 17 MAPKs have been characterized in Arabidopsis and rice respectively, which are used for identification of the putative MAPKs in other higher plants. However, no MAPK gene sequences have yet been characterized for asexually reproducing plants.

In this research, authors from Siksha O Anusandhan University, Bhubaneswar, India describe the analysis of MAPK EST sequences from Curcumalonga (an asexually reproducible plant of great medicinal and economic significance).

The four Curcuma MAPKs contains all 11 MAPK conserved domains and phosphorylation-activation motif, TEY. Phylogenetic analysis grouped them in the subgroup A and C as identified earlier for Arabidopsis. The Curcuma MAPKs identified showed high sequence homology to rice OsMPK3, OsMPK4 and OsMPK5 suggesting the presence of similar key element in signaling biotic and abiotic stress responses. Although further in vivo and in vitro analysis are required to establish the physiological role of Curcuma MAPKs, this study provides the base for future research on diverse signaling pathways mediated by MAPKs in Curcuma longa as well as other asexually reproducing plants.

Authors: Raj Kumar Joshi*, Basudeba Kar, Sanghamitra Nayak.

Source: www.bioinformation.net volume 7(4): 180-183 (2011).

Link: http://www.bioinformation.net/007/97320630007180

Publication date: October 14, 2011.