Probing protein-chromophore interactions in Cph1 phytochrome by mutagenesis.

  title={Probing protein-chromophore interactions in Cph1 phytochrome by mutagenesis.},
  author={Janina Hahn and Holger M. Strauss and Frank T Landgraf and Hortensia Faus Gimen{\`e}z and Guenter Lochnit and Peter Schmieder and Jon Hughes},
  journal={The FEBS journal},
  volume={273 7},
We have investigated mutants of phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803 in order to study chromophore-protein interactions. Cph1Delta2, the 514-residue N-terminal sensor module produced as a recombinant His6-tagged apoprotein in Escherichia coli, autoassembles in vitro to form a holoprotein photochemically indistinguishable from the full-length product. We generated 12 site-directed mutants of Cph1Delta2, focusing on conserved residues which might be involved in… CONTINUE READING
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