Sequence and structural conservation reveal fingerprint residues in TRP channels

  1. Deny Cabezas-Bratesco
  2. Francisco A Mcgee
  3. Charlotte K Colenso
  4. Kattina Zavala
  5. Daniele Granata
  6. Vincenzo Carnevale
  7. Juan C Opazo  Is a corresponding author
  8. Sebastian E Brauchi  Is a corresponding author
  1. Universidad Austral de Chile, Chile
  2. Temple University, United States
  3. University of Bristol, United Kingdom

Abstract

TRP proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the open state in TRP channels are still a matter of debate. Aiming to unveil distinctive structural features common to the transmembrane domains within the TRP family, we performed phylogenetic reconstruction, sequence statistics, and structural analysis over a large set of TRP channel genes. Here we report an exceptionally conserved set of residues. This fingerprint is composed of twelve residues localized at equivalent three-dimensional positions in TRP channels from the different subtypes. Moreover, these amino acids are arranged in three groups, connected by a set of aromatics located at the core of the transmembrane structure. We hypothesize that differences in the connectivity between these different groups of residues harbors the apparent differences in coupling strategies used by TRP subgroups.

Data availability

Sequences, MSA and phylogenetic reconstruction data analyzed during this study are are available in Dryad database: https://doi.org/10.5061/dryad.k6djh9w75Code for analysis of Aromatic Core is available in Github database:https://github.com/brauchilab/ProteinCoreCluster

The following data sets were generated

Article and author information

Author details

  1. Deny Cabezas-Bratesco

    Facultad de Medicina, Universidad Austral de Chile, Valdivia, Chile
    Competing interests
    The authors declare that no competing interests exist.
  2. Francisco A Mcgee

    Department of Biology, Temple University, Philadelphia, United States
    Competing interests
    The authors declare that no competing interests exist.
  3. Charlotte K Colenso

    School of Cellular and Molecular Medicine, University of Bristol, Bristol, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  4. Kattina Zavala

    Instituto de Ciencias Ambientales y Evolutivas, Universidad Austral de Chile, Valdivia, Chile
    Competing interests
    The authors declare that no competing interests exist.
  5. Daniele Granata

    Department of Biology, Temple University, Philadelphia, United States
    Competing interests
    The authors declare that no competing interests exist.
  6. Vincenzo Carnevale

    Department of Biology, Temple University, Philadelphia, United States
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-1918-8280
  7. Juan C Opazo

    Instituto de Ciencias Ambientales y Evolutivas, Universidad Austral de Chile, Valdivia, Chile
    For correspondence
    jopazo@gmail.com
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0001-7938-4083
  8. Sebastian E Brauchi

    Facultad de Medicina, Universidad Austral de Chile, Valdivia, Chile
    For correspondence
    sbrauchi@uach.cl
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-8494-9912

Funding

Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT 3140233)

  • Charlotte K Colenso

Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT 1191868)

  • Sebastian E Brauchi

Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT 1210471)

  • Juan C Opazo

Agencia Nacional de Investigación y Desarrollo (Millennium Science Initiative Program (NCN19_168))

  • Juan C Opazo
  • Sebastian E Brauchi

National Institutes of Health (R01GM093290,S10OD020095,and R01GM131048)

  • Vincenzo Carnevale

National Science Foundation (IOS-1934848)

  • Vincenzo Carnevale

National Science Foundation (1625061)

  • Vincenzo Carnevale

U.S. Army (Research Laboratory W911NF-16-2-0189)

  • Vincenzo Carnevale

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

  1. Andrés Jara-Oseguera, The University of Texas at Austin, United States

Publication history

  1. Received: September 6, 2021
  2. Accepted: May 19, 2022
  3. Accepted Manuscript published: June 10, 2022 (version 1)
  4. Accepted Manuscript updated: June 17, 2022 (version 2)

Copyright

© 2022, Cabezas-Bratesco et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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  1. Deny Cabezas-Bratesco
  2. Francisco A Mcgee
  3. Charlotte K Colenso
  4. Kattina Zavala
  5. Daniele Granata
  6. Vincenzo Carnevale
  7. Juan C Opazo
  8. Sebastian E Brauchi
(2022)
Sequence and structural conservation reveal fingerprint residues in TRP channels
eLife 11:e73645.
https://doi.org/10.7554/eLife.73645

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