Skip to main content
NCBI home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1984 Oct 25;12(20):7949–7959. doi: 10.1093/nar/12.20.7949

Characterization of a halobacterial gene affecting bacterio-opsin gene expression.

M Betlach, J Friedman, H W Boyer, F Pfeifer
PMCID: PMC320221  PMID: 6093059

Abstract

A substantial number of spontaneous bacterio-opsin mutants of Halobacterium halobium are the result of insertion elements up to 1400 bp upstream of the bacterio-opsin (bop) gene. The nucleotide sequence of 1800 bp upstream of the bop gene has been determined. There is a 1118 bp open reading frame (ORF) located within this region which is transcribed and which coincides with the distribution of insertion elements upstream of the bop gene in Bop mutants. Therefore, we propose that there is a gene (brp gene) 526 bp upstream of the bop gene. This putative gene is transcribed in the opposite direction as the bop gene and could encode a protein of 37,500 D (359 amino acids) with a codon usage similar to bacterio-opsin. The 5' terminus of the brp transcript has been determined. The brp transcript and the bop mRNA are complementary for 13 residues near their 5' termini and both transcripts start at or near the initiating codon of the gene. Both transcripts could form similar hairpin loop structures at their 5' termini which contain possible ribosomal binding sites. The DNA sequences immediately upstream of the bop and the brp genes have significant homologies and there is a short complementary sequence. The role of the brp gene in bacterio-opsin gene expression is unclear.

Full text

PDF
7949

Images in this article

7953Image
on p.7953
7955Image
on p.7955

Selected References

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

  1. Betlach M., Pfeifer F., Friedman J., Boyer H. W. Bacterio-opsin mutants of Halobacterium halobium. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1416–1420. doi: 10.1073/pnas.80.5.1416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bina-Stein M., Thoren M., Salzman N., Thomspon J. A. Rapid sequence determination of late simian virus 40 16S mRNA leader by using inhibitors of reverse transcriptase. Proc Natl Acad Sci U S A. 1979 Feb;76(2):731–735. doi: 10.1073/pnas.76.2.731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  4. Dassarma S., Rajbhandary U. L., Khorana H. G. Bacterio-opsin mRNA in wild-type and bacterio-opsin-deficient Halobacterium halobium strains. Proc Natl Acad Sci U S A. 1984 Jan;81(1):125–129. doi: 10.1073/pnas.81.1.125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dunn R., McCoy J., Simsek M., Majumdar A., Chang S. H., Rajbhandary U. L., Khorana H. G. The bacteriorhodopsin gene. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6744–6748. doi: 10.1073/pnas.78.11.6744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Finer-Moore J., Stroud R. M. Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor. Proc Natl Acad Sci U S A. 1984 Jan;81(1):155–159. doi: 10.1073/pnas.81.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henderson R. The purple membrane from Halobacterium halobium. Annu Rev Biophys Bioeng. 1977;6:87–109. doi: 10.1146/annurev.bb.06.060177.000511. [DOI] [PubMed] [Google Scholar]
  8. Kagramanova V. K., Mankin A. S., Baratova L. A., Bogdanov A. A. The 3'-terminal nucleotide sequence of the Halobacterium halobium 16 S rRNA. FEBS Lett. 1982 Jul 19;144(1):177–180. doi: 10.1016/0014-5793(82)80595-4. [DOI] [PubMed] [Google Scholar]
  9. Lee D. C., Roeder R. G. Transcription of adenovirus type 2 genes in a cell-free system: apparent heterogeneity of initiation at some promoters. Mol Cell Biol. 1981 Jul;1(7):635–651. doi: 10.1128/mcb.1.7.635. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  11. Luse D. S., Haynes J. R., VanLeeuwen D., Schon E. A., Cleary M. L., Shapiro S. G., Lingrel J. B., Roeder R. G. Transcription of the beta-like globin genes and pseudogenes of the goat in a cell-free system. Nucleic Acids Res. 1981 Sep 11;9(17):4339–4354. doi: 10.1093/nar/9.17.4339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Madon J., Zillig W. A form of the DNA-dependent RNA polymerase of Halobacterium halobium, containing an additional component, is able to transcribe native DNA. Eur J Biochem. 1983 Jun 15;133(2):471–474. doi: 10.1111/j.1432-1033.1983.tb07487.x. [DOI] [PubMed] [Google Scholar]
  13. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  14. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  15. Moore R. L., McCarthy B. J. Characterization of the deoxyribonucleic acid of various strains of halophilic bacteria. J Bacteriol. 1969 Jul;99(1):248–254. doi: 10.1128/jb.99.1.248-254.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. Pfeifer F., Friedman J., Boyer H. W., Betlach M. Characterization of insertions affecting the expression of the bacterio-opsin gene in Halobacterium halobium. Nucleic Acids Res. 1984 Mar 12;12(5):2489–2497. doi: 10.1093/nar/12.5.2489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pfeifer F., Weidinger G., Goebel W. Genetic variability in Halobacterium halobium. J Bacteriol. 1981 Jan;145(1):375–381. doi: 10.1128/jb.145.1.375-381.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Rüther U., Koenen M., Otto K., Müller-Hill B. pUR222, a vector for cloning and rapid chemical sequencing of DNA. Nucleic Acids Res. 1981 Aug 25;9(16):4087–4098. doi: 10.1093/nar/9.16.4087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. Sumper M., Herrmann G. Biogenesis of purple membrane: regulation of bacterio-opsin synthesis. FEBS Lett. 1976 Oct 15;69(1):149–152. doi: 10.1016/0014-5793(76)80673-4. [DOI] [PubMed] [Google Scholar]
  23. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES