Evidence map›Paper›PMID 11591681›Full record

ArticleJournal of bacteriology2001

An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli.

K H Jung, E N Spudich, V D Trivedi, J L Spudich

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
  3. Article
  4. Article
  5. Review
  6. What site-directed labeling studies tell us about the mechanism of rhodopsin activation and G-protein binding.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2010
    Review
  7. Article
  8. Article
  9. Flexibility of the cytoplasmic domain of the phototaxis transducer II from Natronomonas pharaonis.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2008
    Article
  10. Article
  11. Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Article
  13. Article
  14. A eukaryotic BLUF domain mediates light-dependent gene expression in the purple bacterium Rhodobacter sphaeroides 2.4.1.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  15. Article
  16. Moving fluid with bacterial carpets.Biophysical journal · 2004
    Article
  17. Article
  18. Review
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

4 authors at 1 institution in 1 country.

K H JungDepartment of Microbiology and Molecular Genetics, University of Texas-Houston Medical School, Houston, Texas 77030, USA.
E N Spudich
V D Trivedi
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 R01GM27750
6 · The paper itself

Abstract

Halophilic archaea, such as Halobacterium salinarum and Natronobacterium pharaonis, alter their swimming behavior by phototaxis responses to changes in light intensity and color using visual pigment-like sensory rhodopsins (SRs). In N. pharaonis, SRII (NpSRII) mediates photorepellent responses through its transducer protein, NpHtrII. Here we report the expression of fusions of NpSRII and NpHtrII and fusion hybrids with eubacterial cytoplasmic domains and analyze their function in vivo in haloarchaea and in eubacteria. A fusion in which the C terminus of NpSRII is connected by a short flexible linker to NpHtrII is active in phototaxis signaling for H. salinarum, showing that the fusion does not inhibit functional receptor-transducer interactions. We replaced the cytoplasmic portions of this fusion protein with the cytoplasmic domains of Tar and Tsr, chemotaxis transducers from enteric eubacteria. Purification of the fusion protein from H. salinarum and Tar fusion chimera from Escherichia coli membranes shows that the proteins are not cleaved and exhibit absorption spectra characteristic of wild-type membranes. Their photochemical reaction cycles in H. salinarum and E. coli membranes, respectively, are similar to those of native NpSRII in N. pharaonis. These fusion chimeras mediate retinal-dependent phototaxis responses by Escherichia coli, establishing that the nine-helix membrane portion of the receptor-transducer complex is a modular functional unit able to signal in heterologous membranes. This result confirms a current model for SR-Htr signal transduction in which the Htr transducers are proposed to interact physically and functionally with their cognate sensory rhodopsins via helix-helix contacts between their transmembrane segments.

Indexed as

Escherichia coli ProteinsLightLocomotionReceptors, Cell SurfaceSignal TransductionArchaeal ProteinsBacterial ProteinsCarotenoidsChemoreceptor CellsEscherichia coliHalobacterium salinarumMembrane ProteinsRecombinant Fusion ProteinsTransformation, BacterialArchaeal ProteinsBacterial ProteinsCarotenoidsEscherichia coli ProteinsHtrII protein, Natronobacterium pharaonisMembrane Proteinsphototaxis receptor sensory rhodopsin II, Natronobacterium pharaonisReceptors, Cell SurfaceRecombinant Fusion ProteinsTar protein, E coliTsr protein, Bacteria

Identifiers

PMID11591681
PMCPMC100132
OpenAlexW1972918885

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.