View in EDS

Peroxisomal Δ3,Δ2-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes.

Saved in:
Bibliographic Details
Title: Peroxisomal Δ3,Δ2-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes.
Authors: Goepfert, Simon1,2, Vidoudez, Charles1, Tellgren-Roth, Christian3, Delessert, Syndie1, Hiltunen, J. Kalervo4, Poirier, Yves1 yves.poirier@unil.ch
Source: Plant Journal. Dec2008, Vol. 56 Issue 5, p728-742. 15p. 1 Black and White Photograph, 7 Diagrams, 1 Chart, 2 Graphs.
Subjects: Peroxisomes, Isomerases, Fatty acids, Saccharomyces cerevisiae, Arabidopsis thaliana, Plant cell culture
Abstract: Δ3,Δ2-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the β-oxidation cycle. Three genes encoding Δ3,Δ2-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 have been identified in Arabidopsis thaliana. When expressed heterologously in Saccharomyces cerevisiae, all three ECI proteins were targeted to the peroxisomes and enabled the yeast Δeci1 mutant to degrade 10 Z-heptadecenoic acid, demonstrating Δ3,Δ2-enoyl CoA isomerase activity in vivo. Fusion proteins between yellow fluorescent protein and AtECI1 or AtECI2 were targeted to the peroxisomes in onion epidermal cells and Arabidopsis root cells, but a similar fusion protein with AtECI3 remained in the cytosol for both tissues. AtECI3 targeting to peroxisomes in S. cerevisiae was dependent on yeast PEX5, while expression of Arabidopsis PEX5 in yeast failed to target AtECI3 to peroxisomes. AtECI2 and AtECI3 are tandem duplicated genes and show a high level of amino acid conservation, except at the C-terminus; AtECI2 ends with the well conserved peroxisome targeting signal 1 (PTS1) terminal tripeptide PKL, while AtECI3 possesses a divergent HNL terminal tripeptide. Evolutionary analysis of ECI genes in plants revealed several independent duplication events, with duplications occurring in rice and Medicago truncatula, generating homologues with divergent C-termini and no recognizable PTS1. All plant ECI genes analyzed, including AtECI3, are under negative purifying selection, implying functionality of the cytosolic AtECI3. Analysis of the mammalian and fungal genomes failed to identify cytosolic variants of the Δ3,Δ2-enoyl CoA isomerase, indicating that evolution of cytosolic Δ3,Δ2-enoyl CoA isomerases is restricted to the plant kingdom. [ABSTRACT FROM AUTHOR]
Copyright of Plant Journal is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 35481686
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Peroxisomal Δ<superscript>3</superscript>,Δ<superscript>2</superscript>-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Goepfert%2C+Simon%22">Goepfert, Simon</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Vidoudez%2C+Charles%22">Vidoudez, Charles</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Tellgren-Roth%2C+Christian%22">Tellgren-Roth, Christian</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Delessert%2C+Syndie%22">Delessert, Syndie</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Hiltunen%2C+J%2E+Kalervo%22">Hiltunen, J. Kalervo</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Poirier%2C+Yves%22">Poirier, Yves</searchLink><relatesTo>1</relatesTo><i> yves.poirier@unil.ch</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Plant+Journal%22">Plant Journal</searchLink>. Dec2008, Vol. 56 Issue 5, p728-742. 15p. 1 Black and White Photograph, 7 Diagrams, 1 Chart, 2 Graphs.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Peroxisomes%22">Peroxisomes</searchLink><br /><searchLink fieldCode="DE" term="%22Isomerases%22">Isomerases</searchLink><br /><searchLink fieldCode="DE" term="%22Fatty+acids%22">Fatty acids</searchLink><br /><searchLink fieldCode="DE" term="%22Saccharomyces+cerevisiae%22">Saccharomyces cerevisiae</searchLink><br /><searchLink fieldCode="DE" term="%22Arabidopsis+thaliana%22">Arabidopsis thaliana</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+cell+culture%22">Plant cell culture</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Δ3,Δ2-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the β-oxidation cycle. Three genes encoding Δ3,Δ2-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 have been identified in Arabidopsis thaliana. When expressed heterologously in Saccharomyces cerevisiae, all three ECI proteins were targeted to the peroxisomes and enabled the yeast Δeci1 mutant to degrade 10 Z-heptadecenoic acid, demonstrating Δ3,Δ2-enoyl CoA isomerase activity in vivo. Fusion proteins between yellow fluorescent protein and AtECI1 or AtECI2 were targeted to the peroxisomes in onion epidermal cells and Arabidopsis root cells, but a similar fusion protein with AtECI3 remained in the cytosol for both tissues. AtECI3 targeting to peroxisomes in S. cerevisiae was dependent on yeast PEX5, while expression of Arabidopsis PEX5 in yeast failed to target AtECI3 to peroxisomes. AtECI2 and AtECI3 are tandem duplicated genes and show a high level of amino acid conservation, except at the C-terminus; AtECI2 ends with the well conserved peroxisome targeting signal 1 (PTS1) terminal tripeptide PKL, while AtECI3 possesses a divergent HNL terminal tripeptide. Evolutionary analysis of ECI genes in plants revealed several independent duplication events, with duplications occurring in rice and Medicago truncatula, generating homologues with divergent C-termini and no recognizable PTS1. All plant ECI genes analyzed, including AtECI3, are under negative purifying selection, implying functionality of the cytosolic AtECI3. Analysis of the mammalian and fungal genomes failed to identify cytosolic variants of the Δ3,Δ2-enoyl CoA isomerase, indicating that evolution of cytosolic Δ3,Δ2-enoyl CoA isomerases is restricted to the plant kingdom. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Plant Journal is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=35481686
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1111/j.1365-313X.2008.03635.x
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 15
        StartPage: 728
    Subjects:
      – SubjectFull: Peroxisomes
        Type: general
      – SubjectFull: Isomerases
        Type: general
      – SubjectFull: Fatty acids
        Type: general
      – SubjectFull: Saccharomyces cerevisiae
        Type: general
      – SubjectFull: Arabidopsis thaliana
        Type: general
      – SubjectFull: Plant cell culture
        Type: general
    Titles:
      – TitleFull: Peroxisomal Δ3,Δ2-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Goepfert, Simon
      – PersonEntity:
          Name:
            NameFull: Vidoudez, Charles
      – PersonEntity:
          Name:
            NameFull: Tellgren-Roth, Christian
      – PersonEntity:
          Name:
            NameFull: Delessert, Syndie
      – PersonEntity:
          Name:
            NameFull: Hiltunen, J. Kalervo
      – PersonEntity:
          Name:
            NameFull: Poirier, Yves
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 12
              Text: Dec2008
              Type: published
              Y: 2008
          Identifiers:
            – Type: issn-print
              Value: 09607412
          Numbering:
            – Type: volume
              Value: 56
            – Type: issue
              Value: 5
          Titles:
            – TitleFull: Plant Journal
              Type: main
ResultId 1