Primary Structure of Sensory Rhodopsin I, a Prokaryotic Photoreceptor

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1989 Dec 20

PMID 2591367

Citations 31

Authors

A Blanck

D Oesterhelt

E Ferrando

E S Schegk

F Lottspeich

Affiliations

Soon will be listed here.

Abstract

The gene coding for sensory rhodopsin I (SR-I) has been identified in a restriction fragment of genomic DNA from the Halobacterium halobium strain L33. Of the 1014 nucleotides whose sequence was determined, 720 belong to the structural gene of SR-I. In the 5' non-coding region two putative promoter elements and a ribosomal binding site have been identified. The 3' flanking region bears a potential terminator structure. The SR-I protein moiety carries no signal peptide and is not processed at its N terminus. The C terminus, however, lacks the last aspartic acid residue encoded by the gene. Analysis of the primary structure of SR-I reveals no consistent homology with the eukaryotic photoreceptor rhodopsin, but 14% homology with the halobacterial ion pumps, bacteriorhodopsin (BR) and halorhodopsin (HR). Residues conserved in all three proteins are discussed with respect to their contribution to secondary structure, retinal binding and ion translocation. The aspartic acid residue which mediates in BR the reprotonation of the Schiff base (D96) is replaced in SR-I by a tyrosine (Y87). This amino acid replacement is proposed to be of crucial importance in the evolution of the slow-cycling photosensing pigment SR-I.

Citing Articles

Genome-Wide Identification of G Protein-Coupled Receptors in Ciliated Eukaryotes.

Luo S, Zhang P, Miao W, Xiong J Int J Mol Sci. 2023; 24(4).

PMID: 36835283 PMC: 9960496. DOI: 10.3390/ijms24043869.

Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains.

Mullen L, Boerrigter K, Ferriero N, Rosalsky J, Barrett A, Murray P Front Microbiol. 2018; 9:368.

PMID: 29559961 PMC: 5845674. DOI: 10.3389/fmicb.2018.00368.

Origination of the Protein Fold Repertoire from Oily Pluripotent Peptides.

Mannige R Proteomes. 2017; 2(2):154-168.

PMID: 28250375 PMC: 5302733. DOI: 10.3390/proteomes2020154.

Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins.

Shalaeva D, Galperin M, Mulkidjanian A Biol Direct. 2015; 10:63.

PMID: 26472483 PMC: 4608122. DOI: 10.1186/s13062-015-0091-4.

The signal transfer from the receptor NpSRII to the transducer NpHtrII is not hampered by the D75N mutation.

Holterhues J, Bordignon E, Klose D, Rickert C, Klare J, Martell S Biophys J. 2011; 100(9):2275-82.

PMID: 21539797 PMC: 3149259. DOI: 10.1016/j.bpj.2011.03.017.

References

Reiter W, Palm P, Zillig W . Analysis of transcription in the archaebacterium Sulfolobus indicates that archaebacterial promoters are homologous to eukaryotic pol II promoters. Nucleic Acids Res. 1988; 16(1):1-19. PMC: 334609. DOI: 10.1093/nar/16.1.1. View

Alam M, Oesterhelt D . Morphology, function and isolation of halobacterial flagella. J Mol Biol. 1984; 176(4):459-75. DOI: 10.1016/0022-2836(84)90172-4. View

Hanahan D . Studies on transformation of Escherichia coli with plasmids. J Mol Biol. 1983; 166(4):557-80. DOI: 10.1016/s0022-2836(83)80284-8. View

Oesterhelt D, Hegemann P, Tittor J . The photocycle of the chloride pump halorhodopsin. II: Quantum yields and a kinetic model. EMBO J. 1985; 4(9):2351-6. PMC: 554509. DOI: 10.1002/j.1460-2075.1985.tb03938.x. View

Tittor J, Soell C, Oesterhelt D, Butt H, Bamberg E . A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide. EMBO J. 1989; 8(11):3477-82. PMC: 401504. DOI: 10.1002/j.1460-2075.1989.tb08512.x. View

Spudich E, Hasselbacher C, Spudich J . Methyl-accepting protein associated with bacterial sensory rhodopsin I. J Bacteriol. 1988; 170(9):4280-5. PMC: 211438. DOI: 10.1128/jb.170.9.4280-4285.1988. View

Heijne G . The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 1986; 5(11):3021-7. PMC: 1167256. DOI: 10.1002/j.1460-2075.1986.tb04601.x. View

Clewell D . Nature of Col E 1 plasmid replication in Escherichia coli in the presence of the chloramphenicol. J Bacteriol. 1972; 110(2):667-76. PMC: 247463. DOI: 10.1128/jb.110.2.667-676.1972. View

Heyn M, Westerhausen J, Wallat I, Seiff F . High-sensitivity neutron diffraction of membranes: Location of the Schiff base end of the chromophore of bacteriorhodopsin. Proc Natl Acad Sci U S A. 1988; 85(7):2146-50. PMC: 279946. DOI: 10.1073/pnas.85.7.2146. View

10.

Soppa J, Otomo J, Straub J, Tittor J, Meessen S, Oesterhelt D . Bacteriorhodopsin mutants of Halobacterium sp. GRB. II. Characterization of mutants. J Biol Chem. 1989; 264(22):13049-56. View

11.

de Groot H, Harbison G, Herzfeld J, Griffin R . Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15N shift anisotropy. Biochemistry. 1989; 28(8):3346-53. DOI: 10.1021/bi00434a033. View

12.

KYTE J, Doolittle R . A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982; 157(1):105-32. DOI: 10.1016/0022-2836(82)90515-0. View

13.

Soppa J, Oesterhelt D . Bacteriorhodopsin mutants of Halobacterium sp. GRB. I. The 5-bromo-2'-deoxyuridine selection as a method to isolate point mutants in halobacteria. J Biol Chem. 1989; 264(22):13043-8. View

14.

Hasselbacher C, Spudich J, Dewey T . Circular dichroism of halorhodopsin: comparison with bacteriorhodopsin and sensory rhodopsin I. Biochemistry. 1988; 27(7):2540-6. DOI: 10.1021/bi00407a041. View

15.

Godel H, Graser T, Foldi P, Pfaender P, Furst P . Measurement of free amino acids in human biological fluids by high-performance liquid chromatography. J Chromatogr. 1984; 297:49-61. DOI: 10.1016/s0021-9673(01)89028-2. View

16.

Schegk E, Oesterhelt D . Isolation of a prokaryotic photoreceptor: sensory rhodopsin from halobacteria. EMBO J. 1988; 7(9):2925-33. PMC: 457089. DOI: 10.1002/j.1460-2075.1988.tb03151.x. View

17.

Spudich J, Bogomolni R . Sensory rhodopsins of halobacteria. Annu Rev Biophys Biophys Chem. 1988; 17:193-215. DOI: 10.1146/annurev.bb.17.060188.001205. View

18.

Hackett N, Stern L, Chao B, Kronis K, Khorana H . Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F. J Biol Chem. 1987; 262(19):9277-84. View

19.

Schiffer M, EDMUNDSON A . Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys J. 1967; 7(2):121-35. PMC: 1368002. DOI: 10.1016/S0006-3495(67)86579-2. View

20.

Beato M . Gene regulation by steroid hormones. Cell. 1989; 56(3):335-44. DOI: 10.1016/0092-8674(89)90237-7. View