Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Photochromism of Phytochromes and Cph1 Requires Critical Amino Acids and Secondary Structure in the N-Terminal Domain

  • Seo Hak-Soo (Department of Plant Science, Seoul National University) ;
  • Bhoo Seong-Hee (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University)
  • Published : 2006.09.01
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Abstract

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 ${\alpha}$-helix centered around the residue-391 is in the chromophore pocket and critical for the chromophore ligation.

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References

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