Role of threonine residues in the regulation of manganese-dependent arabidopsis serine/threonine/tyrosine protein kinase activity

Reddy, Mamatha M. ; Rajasekharan, Ram (2006) Role of threonine residues in the regulation of manganese-dependent arabidopsis serine/threonine/tyrosine protein kinase activity Archives of Biochemistry and Biophysics, 455 (2). pp. 99-109. ISSN 0003-9861

Full text not available from this repository.

Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.abb.2006.09.009

Abstract

Tyrosine phosphorylation in plants could be performed only by dual-specificity kinases. Arabidopsis thaliana dual-specificity protein kinase (AtSTYPK) exhibited strong preference for manganese over magnesium for its kinase activity. The kinase autophosphorylated on serine, threonine and tyrosine residues and phosphorylated myelin basic protein on threonine and tyrosine residues. The AtSTYPK harbors manganese dependent serine/threonine kinase domain, COG3642. His248 and Ser265 on COG3642 are conserved in AtSTYPK and the site-directed mutant, H248A showed loss of serine/threonine kinase activity. The protein kinase activity was abolished when Thr208 in the TEY motif and Thr293 of the activation loop were converted to alanine. The conversion of Thr284 in the activation loop to alanine resulted in an increased phosphorylation. This study reports the first identification of a manganese dependent dual-specificity kinase and the importance of Thr208, Thr284, and Thr293 residues in the regulation of kinase activity.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Plant Dual-specificity Protein Kinase; Regulation of Protein Kinase Activity; Site-directed Mutagenesis; MALDI Mass Spectrometry; Protein Phosphorylation
ID Code:55024
Deposited On:17 Aug 2011 12:20
Last Modified:17 Aug 2011 12:20

Repository Staff Only: item control page