Light-Induced Signal Transduction Pathway Involving Inositol Phosphates

Sopory, Sudhir K.; Chandok, Meena R.

doi:10.1007/978-1-4613-0343-5_12

Cited by 7 publications

(1 citation statement)

References 98 publications

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“…Many molecules involved in different signal transduction pathways have been reported. Calcium [1–3], cyclic guanosine monophosphate [4], phosphoinositides [5,6] and other messengers like octadecanoid [7], hydrogen peroxide, salicylic acid [8] and electrical potential [9] play important roles in many physiological processes. One of the most ubiquitous second messengers, calcium, has been shown to be involved in a wide variety of responses in plants which include cold induced gene expression [10], light induced responses [11], self incompatibility [12], rhizobium plant interaction [13], phytohormones [14] and stress [15].…”

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confidence: 99%

A novel protein kinase from Brassica juncea stimulated by a protozoan calcium binding protein

Deswal¹,

Pandey²,

Chandok³

et al. 2000

European Journal of Biochemistry

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A novel protein kinase (BjCCaBPk) from etiolated Brassica juncea seedlings has been purified and partially characterized. The purified enzyme migrated on SDS/PAGE as a single band with an apparent molecular mass of 43 kDa. The optimum pH for the kinase activity was 8.0. It was stimulated more than sixfold by the protozoa Entamoeba histolytica calcium binding protein EhCaBP (10.5 nm) but not by calmodulin (CaM) when used at equimolar concentration. Moreover the kinase also did not bind CaM±Sepharose. There was neither inhibition of the kinase activity in the presence of W-7 (a CaM antagonist), KN-62 (a specific calcium/CaM kinase inhibitor) and anti-CaM Ig, nor any effect on BjCCaBPk activity of staurosporine (a protein kinase C inhibitor). Furthermore a CaM-kinase specific substrate, syntide-2, proved to be a poor substrate for the BjCCaBPk compared with histone III-S. The phosphorylation of histone III-S involved serine residues. Southern and Northern blot analysis showed the presence of EhCaBP homologues in Brassica. The data suggest that BjCCaBPk may be a novel protein kinase with an affinity towards a calcium binding protein like EhCaBP.

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