» Articles » PMID: 11607363

Mutational Analysis of the Structure and Biogenesis of the Photosystem I Reaction Center in the Cyanobacterium Synechocystis Sp. PCC 6803

Overview
Specialty Science
Date 1993 Feb 1
PMID 11607363
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

We have utilized the unicellular cyanobacterium Synechocystis sp. PCC 6803 to incorporate site-directed amino acid substitutions into the photosystem I (PSI) reactioncenter protein PsaB. A cysteine residue (position 565 of PsaB) proposed to serve as a ligand to the [4Fe-4S] center Fx was changed to serine, histidine, and aspartate. These three mutants--C565S, C565H, and C565D--all exhibited greatly reduced accumulation of PSI reaction-center proteins and failed to grow autotrophically, indicating that this cysteine most likely does coordinate Fx, which is crucial for PSI biogenesis. Interestingly, the strain C565S accumulated significantly more PSI than the other two cysteine mutants and displayed photoreduction of the [4Fe-4S] terminal electron acceptors FA and FB. Mutations were also introduced into a leucine zipper motif of PsaB, proposed to participate in reaction-center dimerization. The mutants L522V, L536M, and L522V/L536M all exhibited wild-type characteristics and grew autotrophically, whereas the L522P mutation prevented PSI accumulation. These data do not provide support for a major structural role of the leucine zipper in reaction-center dimerization or in assembly of Fx. However, the amino acid substitutions incorporated were conservative and might not have perturbed the leucine zipper.

Citing Articles

Thermodynamic Factors Controlling Electron Transfer among the Terminal Electron Acceptors of Photosystem I: Insights from Kinetic Modelling.

Santabarbara S, Casazza A Int J Mol Sci. 2024; 25(18).

PMID: 39337283 PMC: 11432928. DOI: 10.3390/ijms25189795.


Systematically ranking the tightness of membrane association for peripheral membrane proteins (PMPs).

Gao L, Ge H, Huang X, Liu K, Zhang Y, Xu W Mol Cell Proteomics. 2014; 14(2):340-53.

PMID: 25505158 PMC: 4350030. DOI: 10.1074/mcp.M114.044800.


Genetic engineering of thylakoid protein complexes by chloroplast transformation in Chlamydomonas reinhardtii.

Webber A, Bingham S, Lee H Photosynth Res. 2013; 44(1-2):191-205.

PMID: 24307038 DOI: 10.1007/BF00018309.


Function and organization of Photosystem I polypeptides.

Chitnis P, Xu Q, Chitnis V, Nechushtai R Photosynth Res. 2013; 44(1-2):23-40.

PMID: 24307023 DOI: 10.1007/BF00018294.


Structure-function studies on the interaction of PsaC with the Photosystem 1 heterodimer : The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803.

Rodday S, Schulz R, McLntosh L, Biggins J Photosynth Res. 2013; 42(3):185-90.

PMID: 24306560 DOI: 10.1007/BF00018261.


References
1.
Manodori A, Cecchini G, Schroder I, Gunsalus R, Werth M, Johnson M . [3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis. Biochemistry. 1992; 31(10):2703-12. DOI: 10.1021/bi00125a010. View

2.
Vieira J, Messing J . The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982; 19(3):259-68. DOI: 10.1016/0378-1119(82)90015-4. View

3.
LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

4.
Ohad N, Hirschberg J . Mutations in the D1 subunit of photosystem II distinguish between quinone and herbicide binding sites. Plant Cell. 1992; 4(3):273-82. PMC: 160128. DOI: 10.1105/tpc.4.3.273. View

5.
Li N, Zhao J, Warren P, Warden J, Bryant D, Golbeck J . PsaD is required for the stable binding of PsaC to the photosystem I core protein of Synechococcus sp. PCC 6301. Biochemistry. 1991; 30(31):7863-72. DOI: 10.1021/bi00245a028. View