Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Oct;76(10):5046–5050. doi: 10.1073/pnas.76.10.5046

Amino acid sequence of bacteriorhodopsin.

H G Khorana, G E Gerber, W C Herlihy, C P Gray, R J Anderegg, K Nihei, K Biemann
PMCID: PMC413076  PMID: 291920

Abstract

The complete primary structure of the purple membrane protein bacteriorhodopsin, which contains 248 amino acid residues, has been determined. Methods used for separation of the hydrophobic fragments included gel permeation and reverse-phase high-pressure liquid chromatography in organic solvents. The amino acid sequence was determined by a combination of automatic Edman degradation and mass spectrometric methods. The total sequence was derived by ordering of the CNBr fragments on the basis of methionine-containing peptides identified by gas chromatographic mass spectrometry and by analysis of N-bromosuccinimide fragments containing overlaps between CNBr fragments. The present sequence differs from that recently reported by Ovchinnikov and coworkers with respect to an additional tryptophan (position 138) and several amino acid assignments.

Full text

PDF
5046

Images in this article

5048Image
on p.5048

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bridgen J., Walker I. D. Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site. Biochemistry. 1976 Feb 24;15(4):792–798. doi: 10.1021/bi00649a010. [DOI] [PubMed] [Google Scholar]
  2. Capaldi R. A., Vanderkooi G. The low polarity of many membrane proteins. Proc Natl Acad Sci U S A. 1972 Apr;69(4):930–932. doi: 10.1073/pnas.69.4.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chou P. Y., Fasman G. D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol. 1978;47:45–148. doi: 10.1002/9780470122921.ch2. [DOI] [PubMed] [Google Scholar]
  4. Gerber G. E., Anderegg R. J., Herlihy W. C., Gray C. P., Biemann K., Khorana H. G. Partial primary structure of bacteriorhodopsin: sequencing methods for membrane proteins. Proc Natl Acad Sci U S A. 1979 Jan;76(1):227–231. doi: 10.1073/pnas.76.1.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gerber G. E., Gray C. P., Wildenauer D., Khorana H. G. Orientation of bacteriorhodopsin in Halobacterium halobium as studied by selective proteolysis. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5426–5430. doi: 10.1073/pnas.74.12.5426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Horn M. J., Laursen R. A. Solid-phase edman degradation: attachment of carboxyl-terminal homoserine peptides to an insoluble resin. FEBS Lett. 1973 Nov 1;36(3):285–288. doi: 10.1016/0014-5793(73)80392-8. [DOI] [PubMed] [Google Scholar]
  7. Keefer L. M., Bradshaw R. A. Structural studies on Halobacterium halobium bacteriorhodopsin. Fed Proc. 1977 May;36(6):1799–1804. [PubMed] [Google Scholar]
  8. Laursen R. A., Horn M. J., Bonner A. G. Solid-phase Edman degradation. The use of p-phenyl diisothiocyanate to attach lysine- and arginine-containing peptides to insoluble resins. FEBS Lett. 1972 Mar;21(1):67–70. doi: 10.1016/0014-5793(72)80165-0. [DOI] [PubMed] [Google Scholar]
  9. Oesterhelt D., Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol. 1971 Sep 29;233(39):149–152. doi: 10.1038/newbio233149a0. [DOI] [PubMed] [Google Scholar]
  10. Ovchinnikov Y. A., Abdulaev N. G., Feigina M. Y., Kiselev A. V., Lobanov N. A. The structural basis of the functioning of bacteriorhodopsin: an overview. FEBS Lett. 1979 Apr 15;100(2):219–224. doi: 10.1016/0014-5793(79)80338-5. [DOI] [PubMed] [Google Scholar]
  11. Ozols J., Gerard C. Covalent structure of the membranous segment of horse cytochrome b5. Chemical cleavage of the native hemoprotein. J Biol Chem. 1977 Dec 10;252(23):8549–8553. [PubMed] [Google Scholar]
  12. Segrest J. P., Feldmann R. J. Membrane proteins: amino acid sequence and membrane penetration. J Mol Biol. 1974 Aug 25;87(4):853–858. doi: 10.1016/0022-2836(74)90090-4. [DOI] [PubMed] [Google Scholar]
  13. Stoeckenius W., Lozier R. H., Bogomolni R. A. Bacteriorhodopsin and the purple membrane of halobacteria. Biochim Biophys Acta. 1979 Mar 14;505(3-4):215–278. doi: 10.1016/0304-4173(79)90006-5. [DOI] [PubMed] [Google Scholar]
  14. Swank R. T., Munkres K. D. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal Biochem. 1971 Feb;39(2):462–477. doi: 10.1016/0003-2697(71)90436-2. [DOI] [PubMed] [Google Scholar]
  15. Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964–2968. doi: 10.1073/pnas.72.8.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Unwin P. N., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol. 1975 May 25;94(3):425–440. doi: 10.1016/0022-2836(75)90212-0. [DOI] [PubMed] [Google Scholar]
  17. Wachter E., Werhahn R. Attachment of tryptophanyl peptides to 3-aminopropyl-glass suited for subsequent solid-phase Edman degradation. Anal Biochem. 1979 Aug;97(1):56–64. doi: 10.1016/0003-2697(79)90327-0. [DOI] [PubMed] [Google Scholar]
  18. Walker J. E., Carne A. F., Schmitt H. W. The topography of the purple membrane. Nature. 1979 Apr 12;278(5705):653–654. doi: 10.1038/278653a0. [DOI] [PubMed] [Google Scholar]
  19. Wickner W. Asymmetric orientation of phage M13 coat protein in Escherichia coli cytoplasmic membranes and in synthetic lipid vesicles. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1159–1163. doi: 10.1073/pnas.73.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES