Literature DB >> 34294052

Identification and characterization of amphibian SLC26A5 using RNA-Seq.

Zhongying Wang1,2,3, Qixuan Wang1,2,3, Hao Wu4,5,6, Zhiwu Huang7,8,9.   

Abstract

BACKGROUND: Prestin (SLC26A5) is responsible for acute sensitivity and frequency selectivity in the vertebrate auditory system. Limited knowledge of prestin is from experiments using site-directed mutagenesis or domain-swapping techniques after the amino acid residues were identified by comparing the sequence of prestin to those of its paralogs and orthologs. Frog prestin is the only representative in amphibian lineage and the studies of it were quite rare with only one species identified.
RESULTS: Here we report a new coding sequence of SLC26A5 for a frog species, Rana catesbeiana (the American bullfrog). In our study, the SLC26A5 gene of Rana has been mapped, sequenced and cloned successively using RNA-Seq. We measured the nonlinear capacitance (NLC) of prestin both in the hair cells of Rana's inner ear and HEK293T cells transfected with this new coding gene. HEK293T cells expressing Rana prestin showed electrophysiological features similar to that of hair cells from its inner ear. Comparative studies of zebrafish, chick, Rana and an ancient frog species showed that chick and zebrafish prestin lacked NLC. Ancient frog's prestin was functionally different from Rana.
CONCLUSIONS: We mapped and sequenced the SLC26A5 of the Rana catesbeiana from its inner ear cDNA using RNA-Seq. The Rana SLC26A5 cDNA was 2292 bp long, encoding a polypeptide of 763 amino acid residues, with 40% identity to mammals. This new coding gene could encode a functionally active protein conferring NLC to both frog HCs and the mammalian cell line. While comparing to its orthologs, the amphibian prestin has been evolutionarily changing its function and becomes more advanced than avian and teleost prestin.
© 2021. The Author(s).

Entities:  

Keywords:  3D protein structure; Amphibian hearing organ; Non-linear capacitance (NLC); Prestin; RNA-Seq; SLC26A5

Mesh:

Substances:

Year:  2021        PMID: 34294052     DOI: 10.1186/s12864-021-07798-6

Source DB:  PubMed          Journal:  BMC Genomics        ISSN: 1471-2164            Impact factor:   3.969


  30 in total

1.  Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein.

Authors:  D Oliver; D Z He; N Klöcker; J Ludwig; U Schulte; S Waldegger; J P Ruppersberg; P Dallos; B Fakler
Journal:  Science       Date:  2001-06-22       Impact factor: 47.728

2.  Limiting dynamics of high-frequency electromechanical transduction of outer hair cells.

Authors:  G Frank; W Hemmert; A W Gummer
Journal:  Proc Natl Acad Sci U S A       Date:  1999-04-13       Impact factor: 11.205

3.  The role of the STAS domain in the function and biogenesis of a sulfate transporter as probed by random mutagenesis.

Authors:  Nakako Shibagaki; Arthur R Grossman
Journal:  J Biol Chem       Date:  2006-06-05       Impact factor: 5.157

4.  Electrokinetic shape changes of cochlear outer hair cells.

Authors:  B Kachar; W E Brownell; R Altschuler; J Fex
Journal:  Nature       Date:  1986 Jul 24-30       Impact factor: 49.962

5.  Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.

Authors:  M Charles Liberman; Jiangang Gao; David Z Z He; Xudong Wu; Shuping Jia; Jian Zuo
Journal:  Nature       Date:  2002-08-28       Impact factor: 49.962

6.  The extracellular loop of pendrin and prestin modulates their voltage-sensing property.

Authors:  Makoto F Kuwabara; Koichiro Wasano; Satoe Takahashi; Justin Bodner; Tomotaka Komori; Sotaro Uemura; Jing Zheng; Tomohiro Shima; Kazuaki Homma
Journal:  J Biol Chem       Date:  2018-05-18       Impact factor: 5.157

7.  The Frequency Response of Outer Hair Cell Voltage-Dependent Motility Is Limited by Kinetics of Prestin.

Authors:  Joseph Santos-Sacchi; Winston Tan
Journal:  J Neurosci       Date:  2018-05-21       Impact factor: 6.167

8.  Chick hair cells do not exhibit voltage-dependent somatic motility.

Authors:  David Z Z He; Kirk W Beisel; Lin Chen; Da-Lian Ding; Shuping Jia; Bernd Fritzsch; Richard Salvi
Journal:  J Physiol       Date:  2003-01-15       Impact factor: 5.182

9.  Structural basis for functional interactions in dimers of SLC26 transporters.

Authors:  Yung-Ning Chang; Eva A Jaumann; Katrin Reichel; Julia Hartmann; Dominik Oliver; Gerhard Hummer; Benesh Joseph; Eric R Geertsma
Journal:  Nat Commun       Date:  2019-05-02       Impact factor: 14.919

10.  Maturation of Voltage-induced Shifts in SLC26a5 (Prestin) Operating Point during Trafficking and Membrane Insertion.

Authors:  Feng Zhai; Lei Song; Jun-Ping Bai; Chunfu Dai; Dhasakumar Navaratnam; Joseph Santos-Sacchi
Journal:  Neuroscience       Date:  2020-02-13       Impact factor: 3.590

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