Characterization of a novel calcium/calmodulin-dependent protein kinase from tobacco

Plant Physiology
Li MaYing-Tang Lu

Abstract

A cDNA encoding a calcium (Ca2+)/calmodulin (CaM)-dependent protein kinase (CaMK) from tobacco (Nicotiana tabacum), NtCaMK1, was isolated by protein-protein interaction-based screening of a cDNA expression library using 35S-labeled CaM as a probe. The genomic sequence is about 24.6 kb, with 21 exons, and the full-length cDNA is 4.8 kb, with an open reading frame for NtCaMK1 consisting of 1,415 amino acid residues. NtCaMK1 has all 11 subdomains of a kinase catalytic domain, lacks EF hands for Ca2+-binding, and is structurally similar to other CaMKs in mammal systems. Biochemical analyses have identified NtCaMK1 as a Ca2+/CaMK since NtCaMK1 phosphorylated itself and histone IIIs as substrate only in the presence of Ca2+/CaM with a Km of 44.5 microm and a Vmax of 416.2 nm min(-1) mg(-1). Kinetic analysis showed that the kinase not previously autophosphorylated had a Km for the synthetic peptide syntide-2 of 22.1 microm and a Vmax of 644.1 nm min(-1) mg(-1) when assayed in the presence of Ca2+/CaM. Once the autophosphorylation of NtCaMK1 was initiated, the phosphorylated form displayed Ca2+/CaM-independent behavior, as many other CaMKs do. Analysis of the CaM-binding domain (CaMBD) in NtCaMK1 with truncated and site-directed mutate...Continue Reading

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Citations

Jun 21, 2005·Biochimica Et Biophysica Acta·Mei ZhangYing-Tang Lu
Aug 3, 2005·Nature Reviews. Molecular Cell Biology·Jeffrey F Harper, Alice Harmon
Feb 6, 2014·The Plant Journal : for Cell and Molecular Biology·Jens HartmannMargret Sauter
Jun 18, 2010·Plant Physiology and Biochemistry : PPB·Nisreen A Al-QuraanNarendra K Singh
Nov 4, 2015·Frontiers in Plant Science·Amardeep S VirdiPrabhjeet Singh
May 10, 2008·The Plant Journal : for Cell and Molecular Biology·Hong-Tao LiuRen-Gang Zhou
Jun 3, 2005·Plant & Cell Physiology·Li-Xiang YangYing-Tang Lu
May 15, 2015·The Journal of Biological Chemistry·Keiichirou NemotoTatsuya Sawasaki

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