Reconstitution of electron transport in photosystem I with PsaC and PsaD proteins expressed in Escherichia coli

Jindong Zhao, Patrick V. Warren, Ning Li, Donald Ashley Bryant, John H. Golbeck

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

A fusion protein, denoted PsaCl, which contains an amino-terminal extension of five amino acids (MEHSM...) and is derived from an in vitro modified form of the psaC gene of Synechococcus sp. PCC 7002, has been over-expressed in Escherichia coli. The product of the psaD gene of Nostoc sp. PCC 8009 has similarly been over-expressed. The PsaCl and PsaD proteins can be combined with the photosystem I core protein of Synechococcus sp. PCC 6301 to reconstitute electron transport from P700 to the terminal FA/FB acceptors. Reconstitution was found to be absolutely dependent on reinsertion of the iron-sulfur clusters in the PsaCI apoprotein and on the presence of the PsaD protein. This implies that the PsaCl holoprotein does not bind solely to the PsaA/PsaB heterodimer but rather that its interaction with these proteins is mediated through the PsaD protein.

Original languageEnglish (US)
Pages (from-to)175-180
Number of pages6
JournalFEBS Letters
Volume276
Issue number1-2
DOIs
StatePublished - Dec 10 1990

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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