Lizard and frog prestin: evolutionary insight into functional changes.

The plasma membrane of mammalian cochlear outer hair cells contains prestin, a unique motor protein. Prestin is the fifth member of the solute carrier protein 26A family. Orthologs of prestin are also found in the ear of non-mammalian vertebrates such as zebrafish and chicken. However, these ortholo...

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Main Authors: Jie Tang, Jason L Pecka, Bernd Fritzsch, Kirk W Beisel, David Z Z He
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3546999?pdf=render
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spelling doaj-b7d371176d194df98f4931c899421dbe2020-11-25T01:53:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0181e5438810.1371/journal.pone.0054388Lizard and frog prestin: evolutionary insight into functional changes.Jie TangJason L PeckaBernd FritzschKirk W BeiselDavid Z Z HeThe plasma membrane of mammalian cochlear outer hair cells contains prestin, a unique motor protein. Prestin is the fifth member of the solute carrier protein 26A family. Orthologs of prestin are also found in the ear of non-mammalian vertebrates such as zebrafish and chicken. However, these orthologs are electrogenic anion exchangers/transporters with no motor function. Amphibian and reptilian lineages represent phylogenic branches in the evolution of tetrapods and subsequent amniotes. Comparison of the peptide sequences and functional properties of these prestin orthologs offer new insights into prestin evolution. With the recent availability of the lizard and frog genome sequences, we examined amino acid sequence and function of lizard and frog prestins to determine how they are functionally and structurally different from prestins of mammals and other non-mammals. Somatic motility, voltage-dependent nonlinear capacitance (NLC), the two hallmarks of prestin function, and transport capability were measured in transfected human embryonic kidney cells using voltage-clamp and radioisotope techniques. We demonstrated that while the transport capability of lizard and frog prestin was compatible to that of chicken prestin, the NLC of lizard prestin was more robust than that of chicken's and was close to that of platypus. However, unlike platypus prestin which has acquired motor capability, lizard or frog prestin did not demonstrate motor capability. Lizard and frog prestins do not possess the same 11-amino-acid motif that is likely the structural adaptation for motor function in mammals. Thus, lizard and frog prestins appear to be functionally more advanced than that of chicken prestin, although motor capability is not yet acquired.http://europepmc.org/articles/PMC3546999?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Jie Tang
Jason L Pecka
Bernd Fritzsch
Kirk W Beisel
David Z Z He
spellingShingle Jie Tang
Jason L Pecka
Bernd Fritzsch
Kirk W Beisel
David Z Z He
Lizard and frog prestin: evolutionary insight into functional changes.
PLoS ONE
author_facet Jie Tang
Jason L Pecka
Bernd Fritzsch
Kirk W Beisel
David Z Z He
author_sort Jie Tang
title Lizard and frog prestin: evolutionary insight into functional changes.
title_short Lizard and frog prestin: evolutionary insight into functional changes.
title_full Lizard and frog prestin: evolutionary insight into functional changes.
title_fullStr Lizard and frog prestin: evolutionary insight into functional changes.
title_full_unstemmed Lizard and frog prestin: evolutionary insight into functional changes.
title_sort lizard and frog prestin: evolutionary insight into functional changes.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description The plasma membrane of mammalian cochlear outer hair cells contains prestin, a unique motor protein. Prestin is the fifth member of the solute carrier protein 26A family. Orthologs of prestin are also found in the ear of non-mammalian vertebrates such as zebrafish and chicken. However, these orthologs are electrogenic anion exchangers/transporters with no motor function. Amphibian and reptilian lineages represent phylogenic branches in the evolution of tetrapods and subsequent amniotes. Comparison of the peptide sequences and functional properties of these prestin orthologs offer new insights into prestin evolution. With the recent availability of the lizard and frog genome sequences, we examined amino acid sequence and function of lizard and frog prestins to determine how they are functionally and structurally different from prestins of mammals and other non-mammals. Somatic motility, voltage-dependent nonlinear capacitance (NLC), the two hallmarks of prestin function, and transport capability were measured in transfected human embryonic kidney cells using voltage-clamp and radioisotope techniques. We demonstrated that while the transport capability of lizard and frog prestin was compatible to that of chicken prestin, the NLC of lizard prestin was more robust than that of chicken's and was close to that of platypus. However, unlike platypus prestin which has acquired motor capability, lizard or frog prestin did not demonstrate motor capability. Lizard and frog prestins do not possess the same 11-amino-acid motif that is likely the structural adaptation for motor function in mammals. Thus, lizard and frog prestins appear to be functionally more advanced than that of chicken prestin, although motor capability is not yet acquired.
url http://europepmc.org/articles/PMC3546999?pdf=render
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