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

Jindong Zhao; Patrick V. Warren; Ning Li; Donald A. Bryant; John H. Golbeck

doi:10.1016/0014-5793(90)80536-R

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

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

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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 F_A/F_B 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 language	English (US)
Pages (from-to)	175-180
Number of pages	6
Journal	FEBS Letters
Volume	276
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)80536-R
State	Published - Dec 10 1990

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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@article{9d49ea7e45804389a939f8ca194364f6,

title = "Reconstitution of electron transport in photosystem I with PsaC and PsaD proteins expressed in Escherichia coli",

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.",

author = "Jindong Zhao and Warren, {Patrick V.} and Ning Li and Bryant, {Donald A.} and Golbeck, {John H.}",

note = "Funding Information: Acknowledgements: This work was supported by grants DMB-890506t.5o J.H.G. and DMB-881899t7o D.A.B. from the National ScienceF oundation.The authorst hank Drs J. Brosius and F.W. Studierf or plasmidsa ndE. coli strains,a nd Dr GuatamS arath for performingt he amino acid sequencing.",

year = "1990",

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doi = "10.1016/0014-5793(90)80536-R",

language = "English (US)",

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T1 - Reconstitution of electron transport in photosystem I with PsaC and PsaD proteins expressed in Escherichia coli

AU - Zhao, Jindong

AU - Warren, Patrick V.

AU - Li, Ning

AU - Bryant, Donald A.

AU - Golbeck, John H.

N1 - Funding Information: Acknowledgements: This work was supported by grants DMB-890506t.5o J.H.G. and DMB-881899t7o D.A.B. from the National ScienceF oundation.The authorst hank Drs J. Brosius and F.W. Studierf or plasmidsa ndE. coli strains,a nd Dr GuatamS arath for performingt he amino acid sequencing.

PY - 1990/12/10

Y1 - 1990/12/10

N2 - 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.

AB - 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.

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

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