Expression of recombinant full-length plant phytochromes assembled with phytochromobilin in Pichia pastoris

FEBS Lett. 2014 Aug 25;588(17):2964-70. doi: 10.1016/j.febslet.2014.05.050. Epub 2014 Jun 6.

Abstract

We have successfully developed a system to produce full-length plant phytochrome assembled with phytochromobilin in Pichia pastoris by co-expressing apophytochromes and chromophore biosynthetic genes, heme oxygenase (HY1) and phytochromobilin synthase (HY2) from Arabidopsis. Affinity-purified phytochrome proteins from Pichia cells displayed zinc fluorescence indicating chromophore attachment. Spectroscopic analyses showed absorbance maximum peaks identical to in vitro reconstituted phytochromobilin-assembled phytochromes, suggesting that the co-expression system is effective to generate holo-phytochromes. Moreover, mitochondria localization of the phytochromobilin biosynthetic genes increased the efficiency of holophytochrome biosynthesis. Therefore, this system provides an excellent source of holophytochromes, including oat phytochrome A and Arabidopsis phytochrome B.

Keywords: Bilin reductase; Chromophore; Heme oxygenase; Holophytochrome; Phytochromobilin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Apoproteins / biosynthesis
  • Apoproteins / chemistry
  • Apoproteins / genetics
  • Apoproteins / metabolism
  • Biliverdine / analogs & derivatives*
  • Biliverdine / metabolism
  • Gene Expression
  • Genetic Engineering / methods*
  • Heme Oxygenase-1 / genetics
  • Mitochondria / metabolism
  • Molecular Sequence Data
  • Phytochrome / biosynthesis
  • Phytochrome / chemistry
  • Phytochrome / genetics*
  • Phytochrome / metabolism*
  • Pichia / genetics*
  • Protein Transport
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics*
  • Recombinant Proteins / metabolism*

Substances

  • Apoproteins
  • Recombinant Proteins
  • Phytochrome
  • phytochromobilin
  • Heme Oxygenase-1
  • Biliverdine