Evidence map›Paper›PMID 9555883›Full record

ArticleJournal of bacteriology1998

Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism.

K H Jung, J L Spudich

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Gating mechanisms of a natural anion channelrhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  10. Review
  11. A Schiff base connectivity switch in sensory rhodopsin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  12. Article
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  20. 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
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

2 authors at 1 institution in 1 country.

K H JungDepartment of Microbiology and Molecular Genetics, University of Texas-Houston Medical School, 77030, USA.
J L Spudich
The University of Texas Health Science Center at Houston · 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

The molecular complex containing the phototaxis receptor sensory rhodopsin I (SRI) and transducer protein HtrI (halobacterial transducer for SRI) mediates color-sensitive phototaxis responses in the archaeon Halobacterium salinarum. One-photon excitation of the complex by orange light elicits attractant responses, while two-photon excitation (orange followed by near-UV light) elicits repellent responses in swimming cells. Several mutations in SRI and HtrI cause an unusual mutant phenotype, called orange-light-inverted signaling, in which the cell produces a repellent response to normally attractant light. We applied a selection procedure for intragenic and extragenic suppressors of orange-light-inverted mutants and identified 15 distinct second-site mutations that restore the attractant response. Two of the 3 suppressor mutations in SRI are positioned at the cytoplasmic ends of helices F and G, and 12 suppressor mutations in HtrI cluster at the cytoplasmic end of the second HtrI transmembrane helix (TM2). Nearly all suppressors invert the normally repellent response to two-photon stimulation to an attractant response when they are expressed with their suppressible mutant alleles or in an otherwise wild-type strain. The results lead to a model for control of flagellar reversal by the SRI-HtrI complex. The model invokes an equilibrium between the A (reversal-inhibiting) and R (reversal-stimulating) conformers of the signaling complex. Attractant light and repellent light shift the equilibrium toward the A and R conformers, respectively, and mutations are proposed to cause intrinsic shifts in the equilibrium in the dark form of the complex. Differences in the strength of the two-photon signal inversion and in the allele specificity of suppression are correlated, and this correlation can be explained in terms of different values of the equilibrium constant (Keq) for the conformational transition in different mutants and mutant-suppressor pairs.

Indexed as

Archaeal ProteinsHalorhodopsinsProtein Structure, SecondarySensory RhodopsinsBacterial ProteinsBacteriorhodopsinsCell MovementColorDarknessFlagellaHalobacterium salinarumLightMembrane ProteinsModels, MolecularMutagenesis, Site-DirectedPhenotypeArchaeal ProteinsBacterial ProteinsBacteriorhodopsinsHalorhodopsinshtrI protein, Halobacterium salinariumMembrane ProteinsRecombinant ProteinsSensory RhodopsinsSRI protein, Halobacterium

Identifiers

PMID9555883
PMCPMC107127
OpenAlexW2170996281

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.