Stable complex formation of thylakoidal processing peptidase and PGRL1

FEBS Lett. 2013 Jul 11;587(14):2226-31. doi: 10.1016/j.febslet.2013.05.050. Epub 2013 May 31.

Abstract

The thylakoid-transfer signal is required for energy-dependent translocation of preproteins into the thylakoid lumen and is removed by the thylakoidal processing peptidase (TPP). PGRL1 is an essential component of antimycin A-sensitive photosynthetic cyclic electron flow in chloroplasts. Here we report that one of the TPP isoforms, Plsp1, forms a stable complex with PGRL1. Genetic data demonstrate that PGRL1 is not essential for Plsp1 activity in vivo, leading to a possibility that PGRL1 may act as a regulator of TPP.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis / growth & development
  • Arabidopsis Proteins / metabolism*
  • Enzyme Stability
  • Genes, Lethal
  • Membrane Proteins / metabolism*
  • Multiprotein Complexes / metabolism
  • Protein Multimerization
  • Seedlings / enzymology*
  • Seedlings / genetics
  • Seedlings / growth & development
  • Serine Endopeptidases / metabolism*
  • Thylakoids / enzymology*
  • Thylakoids / physiology

Substances

  • Arabidopsis Proteins
  • Membrane Proteins
  • Multiprotein Complexes
  • PGRL1 protein, Arabidopsis
  • Serine Endopeptidases
  • PLSP1 protein, Arabidopsis