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Williams JC, Steiner LA, Ogden RC, et al. Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1983;80(21):6505-9doi: 10.1073/pnas.80.21.6505.
Williams, J. C., Steiner, L. A., Ogden, R. C., Simon, M. I., & Feher, G. (1983). Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides. Proceedings of the National Academy of Sciences of the United States of America, 80(21), 6505-9. https://doi.org/10.1073/pnas.80.21.6505
Williams, J C, et al. "Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides." Proceedings of the National Academy of Sciences of the United States of America vol. 80,21 (1983): 6505-9. doi: https://doi.org/10.1073/pnas.80.21.6505
Williams JC, Steiner LA, Ogden RC, Simon MI, Feher G. Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6505-9. doi: 10.1073/pnas.80.21.6505. PMID: 16593385; PMCID: PMC390381.
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Proc Natl Acad Sci U S A. 1983 Nov;80(21):6505-9. doi: 10.1073/pnas.80.21.6505.

Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides.

Proceedings of the National Academy of Sciences of the United States of America

J C Williams, L A Steiner, R C Ogden, M I Simon, G Feher

Affiliations

  1. Department of Biology, University of California, San Diego, La Jolla, CA 92093.

PMID: 16593385 PMCID: PMC390381 DOI: 10.1073/pnas.80.21.6505

Abstract

The reaction center is a membrane-bound bacteriochlorophyll-protein complex that mediates the primary photochemical events in the photosynthetic bacterium Rhodopseudomonas sphaeroides. The previously determined amino-terminal sequences of the three subunits of the reaction center protein were used to design synthetic mixed oligonucleotide probes for the structural genes encoding the subunits. One of these probes was used to isolate and clone a fragment of DNA from R. sphaeroides that contained the gene encoding the M subunit. The nucleotide sequence of this gene was determined by the dideoxy method. In addition, a number of tryptic and chymotryptic peptides from the M protein were isolated and subjected to sequence analysis, and the sequence of the carboxyl terminus was determined. Together with the amino-terminal sequence, the data establish the primary structure of the M protein. The distribution of hydrophobic residues in the amino acid sequence suggests the presence of five membrane-spanning segments. A significant homology was found between the amino acid sequence of the M subunit and a thylakoid membrane protein (M(r) 32,000) from spinach that has been implicated in herbicide and quinone binding.

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