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KMID : 0545120060160091441
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Journal of Microbiology and Biotechnology
2006 Volume.16 No. 9 p.1441 ~ p.1447
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Photochromism of Phytochromes and Cph1 Requires Critical Amino Acids and Secondary Structure in the N-Terminal Domain
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Seo Hak-Soo
Bhoo Seong-Hee
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Abstract
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The light perception and phototransformation of phytochromes are the first process of the phytochrome-mediated light signal transduction. The chromophore ligation and its photochromism of various site-specific and deletion mutants of pea phytochrome A and bacterial phytochrome-like protein (Cph1) were analyzed in vitro. Serial truncation mutants from the N-terminus and C-terminus indicated that the minimal N-terminal domain for the chromophore ligation spans from the residue 78 to 399 of pea phytochrome A. Site-specific mutants indicated that several residues are critical for the chromophore ligation and/or photochromism. Histidine-324 appears to serve as an anchimeric residue for photochromism through its H-bonding function. Isoleucine-80 and arginine-383 playa critical role for the chromophore ligation and photochromism. Arginine-383 is presumably involved in the stabilization of the Pfr form of pea phytochrome A. Apparently, the amphiphilic -helix centered around the residue-391 is in the chromophore pocket and critical for the chromophore ligation.
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KEYWORD
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zinc-blot, Phytochromes, photochromism, chromophore, Cph1
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