Biosynthesis of open-chain tetrapyrroles in Prochlorococcus marinus

FEMS Microbiol Lett. 2007 Jun;271(2):251-7. doi: 10.1111/j.1574-6968.2007.00715.x. Epub 2007 Apr 17.

Abstract

Members of the genus Prochlorococcus belong to the most abundant phytoplankton on earth. In contrast to other cyanobacteria, Prochlorococcus is characterized by divinyl-chlorophyll containing light-harvesting complexes and the lack of phycobilisomes. Despite the lack of phycobilisomes, all sequenced genomes of Prochlorococcus possess genes that putatively encode enzymes involved in the biosynthesis of open-chain tetrapyrrole molecules. Here, biochemical evidence is presented indicating that high-light- and low-light-adapted Prochlorococcus ecotypes possess genes encoding functional enzymes for the biosynthesis of open-chain tetrapyrrole molecules. Experiments on recombinant protein as well as through complementation studies of a cyanobacterial insertion mutant revealed the functionality of the bilin reductases investigated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bile Pigments / biosynthesis
  • Bile Pigments / chemistry
  • Chromatography, High Pressure Liquid
  • Genetic Complementation Test
  • Light
  • Light-Harvesting Protein Complexes / biosynthesis
  • Light-Harvesting Protein Complexes / chemistry
  • Models, Biological
  • Molecular Structure
  • Mutation
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism
  • Phycoerythrin / biosynthesis
  • Phycoerythrin / chemistry
  • Phylogeny
  • Plasmids / genetics
  • Prochlorococcus / genetics
  • Prochlorococcus / metabolism*
  • Prochlorococcus / radiation effects
  • Recombinant Proteins / metabolism
  • Spectrophotometry
  • Tetrapyrroles / biosynthesis*
  • Tetrapyrroles / chemistry

Substances

  • Bile Pigments
  • Light-Harvesting Protein Complexes
  • Recombinant Proteins
  • Tetrapyrroles
  • Phycoerythrin
  • Oxidoreductases