Sequence similarities of phytochrome to protein kinases: implication for the structure, function and evolution of the phytochrome gene family

FEBS Letters

Thümmler, Fritz²  Algarra, Patricia²  Fobo, Gisela M.¹ 

[1] Martinsried Institute for Protein Sequences (MIPS) am Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried bei München, Germany;Botanisches Institut der Universität München, Menzingerstr.67, D-80638 München, Germany

关键词: Multiple sequence alignment;    Phosphorylation;    Plant signal transduction;    Plant photoreceptor;    Sequence conservation;    Histidine kinase;   

DOI  :  10.1016/0014-5793(94)01327-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phytochrome, the best characterised plant photoreceptor, is encoded by a small multigene family within the plant kingdom. The different phytochrome types are composed of a conserved light-sensing chromophore domain of about 80 kDa and a less-conserved C-terminal domain of about 50 kDa. The C-terminus of phytochrome of the moss Ceratodon purpureus is homologous to the catalytic domain of eukaryotic serine/threonine or tyrosine protein kinases; in contrast, for all other phytochromes (conventional phytochromes) sequence similarities within the C-terminal domain to the catalytic domain of bacterial histidine kinases have been reported. We performed careful sequence comparisons of the putative catalytic domains of phytochrome with each other, with authentic serine/threonine, tyrosine and with histidine kinases. We report that conventional phytochromes exhibit structural elements of the catalytic domains of both histidine and, to a lesser extent, of serine/threonine and tyrosine kinases. The significance of these observations is discussed in the framework of the structure, function and evolution of phytochrome.

【 授权许可】

Unknown