Evidence map›Paper›PMID 7708770›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II.

R Seidel, B Scharf, M Gautel, K Kleine, D Oesterhelt, M Engelhard

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Molecular Biology of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  3. High-resolution structural insights into the heliorhodopsin family.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Taxis in archaea.Emerging topics in life sciences · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Article
  13. Article
  14. Computational analysis of the transient movement of helices in sensory rhodopsin II.Protein science : a publication of the Protein Society · 2005
    Article
  15. Article
  16. Article
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  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

R SeidelMax-Planck-Institut für Molekulare Physiologie, Dortmund, Germany.
B Scharf
M Gautel
K Kleine
D Oesterhelt
M Engelhard
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The blue-light receptor genes (sopII) of sensory rhodopsin (SR) II were cloned from two species, the halophilic bacteria Haloarcula vallismortis (vSR-II) and Natronobacterium pharaonis (pSR-II). Upstream of both sopII gene loci, sequences corresponding to the halobacterial transducer of rhodopsin (Htr) II were recognized. In N. pharaonis, psopII and phtrII are transcribed as a single transcript. Comparison of the amino acid sequences of vHtr-II and pHtr-II with Htr-I and the chemotactic methyl-accepting proteins from Escherichia coli revealed considerable identities in the signal domain and methyl-accepting sites. Similarities with Htr-I in Halobacterium salinarium suggest a common principle in the phototaxis of extreme halophiles. Alignment of all known retinal protein sequences from Archaea identifies both SR-IIs as an additional subgroup of the family. Positions defining the retinal binding site are usually identical with the exception of Met-118 (numbering is according to the bacteriorhodopsin sequence), which might explain the typical blue color shift of SR-II to approximately 490 nm. In archaeal retinal proteins, the function can be deduced from amino acids in positions 85 and 96. Proton pumps are characterized by Asp-85 and Asp-96; chloride pumps by Thr-85 and Ala-96; and sensors by Asp-85 and Tyr-96 or Phe-96.

Indexed as

Archaeal ProteinsCarotenoidsHalorhodopsinsSensory RhodopsinsAmino Acid SequenceArchaeaBacteriorhodopsinsBase SequenceBlotting, SouthernCloning, MolecularDNA, BacterialDNA PrimersGenes, BacterialGenomic LibraryHalobacterialesHalobacteriumArchaeal ProteinsBacteriorhodopsinsCarotenoidsDNA, BacterialDNA PrimersHalorhodopsinssensory rhodopsin II protein, archaealSensory Rhodopsins

Identifiers

PMID7708770
PMCPMC42354
OpenAlexW2043288597

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.