NdhV Is a Subunit of NADPH Dehydrogenase Essential for Cyclic Electron Transport in Synechocystis sp. Strain PCC 6803

Plant Physiol. 2016 Feb;170(2):752-60. doi: 10.1104/pp.15.01430. Epub 2015 Dec 7.

Abstract

Two mutants sensitive to heat stress for growth and impaired in NADPH dehydrogenase (NDH-1)-dependent cyclic electron transport around photosystem I (NDH-CET) were isolated from the cyanobacterium Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in the same sll0272 gene, encoding a protein highly homologous to NdhV identified in Arabidopsis (Arabidopsis thaliana). Deletion of the sll0272 gene (ndhV) did not influence the assembly of NDH-1 complexes and the activities of CO2 uptake and respiration but reduced the activity of NDH-CET. NdhV interacted with NdhS, a ferredoxin-binding subunit of cyanobacterial NDH-1 complex. Deletion of NdhS completely abolished NdhV, but deletion of NdhV had no effect on the amount of NdhS. Reduction of NDH-CET activity was more significant in ΔndhS than in ΔndhV. We therefore propose that NdhV cooperates with NdhS to accept electrons from reduced ferredoxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Carbon Dioxide / metabolism
  • Electron Transport
  • Ferredoxins / metabolism
  • Models, Molecular*
  • Mutation
  • NADPH Dehydrogenase / chemistry
  • NADPH Dehydrogenase / genetics
  • NADPH Dehydrogenase / metabolism*
  • Photosystem I Protein Complex / metabolism
  • Protein Binding
  • Protein Domains
  • Protein Subunits
  • Sequence Deletion
  • Synechocystis / enzymology*
  • Synechocystis / genetics

Substances

  • Bacterial Proteins
  • Ferredoxins
  • Photosystem I Protein Complex
  • Protein Subunits
  • Carbon Dioxide
  • NADPH Dehydrogenase