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Sequence similarities of phytochrome to protein kinases: implication for the structure, function and evolution of the phytochrome gene family
Author(s) -
Thümmler Fritz,
Algarra Patricia,
Fobo Gisela M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01327-w
Subject(s) - phytochrome , biology , hamp domain , histidine , serine , biochemistry , threonine , conserved sequence , phytochrome a , kinase , peptide sequence , phosphorylation , microbiology and biotechnology , gene , arabidopsis , amino acid , botany , red light , mutant
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.