Evidence map›Paper›PMID 9927658›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices.

X N Zhang, J Zhu, J L Spudich

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Computational analysis of the transient movement of helices in sensory rhodopsin II.Protein science : a publication of the Protein Society · 2005
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. X-ray structure of sensory rhodopsin II at 2.1-A resolution.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  14. Article
  15. Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  16. Article
  17. Review
  18. Review
  19. Article
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

3 authors at 1 institution in 1 country.

X N ZhangDepartment of Microbiology and Molecular Genetics, The University of Texas Medical School, Houston, TX 77030, USA.
J Zhu
J L Spudich
The University of Texas at Austin · US

Funding

Structure/Function of Microbial Sensory RhodopsinsR01GM027750 · NIGMS · YESHIVA UNIVERSITY · PI SPUDICH, JOHN LEE · 1985 to 2020
$6.6M
NIGMS NIH HHS R01 GM027750NIGMS NIH HHS R01-GM27750
6 · The paper itself

Abstract

Chimeras of the Halobacterium salinarum transducers HtrI and HtrII were constructed to study the structural determinants for their specific interaction with the phototaxis receptors sensory rhodopsins I and II (SRI and SRII), respectively. Interaction of receptors and transducers was assessed by two criteria: phototaxis responses by the cells and transducer-modulation of receptor photochemical reaction kinetics in membranes. Coexpression of HtrI with SRII or HtrII with SRI did not result in interaction by either criterion. Each receptor was coexpressed with chimeric transducers in which various domains of the two transducers were interchanged. The results show that the presence of the two transmembrane helices of HtrI in a chimera is necessary and sufficient for functional transducer complexation with SRI, i.e., for wild-type SRI photoreactions and attractant and 2-photon repellent phototaxis responses. Additionally, a previously demonstrated chaperone-like facilitation of SRI folding or stability by HtrI was shown to depend only on the two transmembrane helices of HtrI in chimeric transducers. Similarly, the two transmembrane helices of HtrII specify interaction with the repellent receptor SRII according to motility analysis and laser-flash spectroscopy. The results support a model in which the membrane domains of the receptor/transducer complexes, consisting of the seven helices of the receptor interacting with the four-helix bundle of the transducer dimer, produce SRI- and SRII-specific signals to the flagellar motor by means of interchangeable cytoplasmic domains.

Indexed as

Archaeal ProteinsCarotenoidsHalorhodopsinsProtein Structure, SecondarySensory RhodopsinsBacterial ProteinsBacteriorhodopsinsCell MembraneHalobacterium salinarumKineticsLightMembrane ProteinsMovementRecombinant Fusion ProteinsSignal TransductionTime FactorsArchaeal ProteinsBacterial ProteinsBacteriorhodopsinsCarotenoidsHalorhodopsinsHtrII protein, Halobacterium salinariumhtrI protein, Halobacterium salinariumMembrane ProteinsRecombinant Fusion Proteinssensory rhodopsin II protein, archaealSensory RhodopsinsSRI protein, Halobacterium

Identifiers

PMID9927658
PMCPMC15315
OpenAlexW1998476427

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.