View in EDS PDF Full Text

Localization and functionality of microsporidian iron–sulphur cluster assembly proteins.

Saved in:
Bibliographic Details
Title: Localization and functionality of microsporidian iron–sulphur cluster assembly proteins.
Authors: Goldberg, Alina V., Molik, Sabine, Tsaousis, Anastasios D., Neumann, Karina, Kuhnke, Grit, Delbac, Frederic, Vivares, Christian P., Hirt, Robert P., Lill, Roland, Embley, T. Martin
Source: Nature. 4/3/2008, Vol. 452 Issue 7187, p624-628. 5p. 2 Color Photographs, 2 Graphs.
Subjects: Microsporidia, Intracellular pathogens, Biomarkers, Mitochondria, Proteins, Nosema cuniculi, Aerobic bacteria, Biosynthesis, Sulfur compounds
Abstract: Microsporidia are highly specialized obligate intracellular parasites of other eukaryotes (including humans) that show extreme reduction at the molecular, cellular and biochemical level. Although microsporidia have long been considered as early branching eukaryotes that lack mitochondria, they have recently been shown to contain a tiny mitochondrial remnant called a mitosome. The function of the mitosome is unknown, because microsporidians lack the genes for canonical mitochondrial functions, such as aerobic respiration and haem biosynthesis. However, microsporidial genomes encode several components of the mitochondrial iron–sulphur (Fe–S) cluster assembly machinery. Here we provide experimental insights into the metabolic function and localization of these proteins. We cloned, functionally characterized and localized homologues of several central mitochondrial Fe–S cluster assembly components for the microsporidians Encephalitozoon cuniculi and Trachipleistophora hominis. Several microsporidial proteins can functionally replace their yeast counterparts in Fe–S protein biogenesis. In E. cuniculi, the iron (frataxin) and sulphur (cysteine desulphurase, Nfs1) donors and the scaffold protein (Isu1) co-localize with mitochondrial Hsp70 to the mitosome, consistent with it being the functional site for Fe–S cluster biosynthesis. In T. hominis, mitochondrial Hsp70 and the essential sulphur donor (Nfs1) are still in the mitosome, but surprisingly the main pools of Isu1 and frataxin are cytosolic, creating a conundrum of how these key components of Fe–S cluster biosynthesis coordinate their function. Together, our studies identify the essential biosynthetic process of Fe–S protein assembly as a key function of microsporidian mitosomes. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature 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: Psychology and Behavioral Sciences Collection
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: pbh
DbLabel: Psychology and Behavioral Sciences Collection
An: 31514383
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Localization and functionality of microsporidian iron–sulphur cluster assembly proteins.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Goldberg%2C+Alina+V%2E%22">Goldberg, Alina V.</searchLink><br /><searchLink fieldCode="AR" term="%22Molik%2C+Sabine%22">Molik, Sabine</searchLink><br /><searchLink fieldCode="AR" term="%22Tsaousis%2C+Anastasios+D%2E%22">Tsaousis, Anastasios D.</searchLink><br /><searchLink fieldCode="AR" term="%22Neumann%2C+Karina%22">Neumann, Karina</searchLink><br /><searchLink fieldCode="AR" term="%22Kuhnke%2C+Grit%22">Kuhnke, Grit</searchLink><br /><searchLink fieldCode="AR" term="%22Delbac%2C+Frederic%22">Delbac, Frederic</searchLink><br /><searchLink fieldCode="AR" term="%22Vivares%2C+Christian+P%2E%22">Vivares, Christian P.</searchLink><br /><searchLink fieldCode="AR" term="%22Hirt%2C+Robert+P%2E%22">Hirt, Robert P.</searchLink><br /><searchLink fieldCode="AR" term="%22Lill%2C+Roland%22">Lill, Roland</searchLink><br /><searchLink fieldCode="AR" term="%22Embley%2C+T%2E+Martin%22">Embley, T. Martin</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 4/3/2008, Vol. 452 Issue 7187, p624-628. 5p. 2 Color Photographs, 2 Graphs.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Microsporidia%22">Microsporidia</searchLink><br /><searchLink fieldCode="DE" term="%22Intracellular+pathogens%22">Intracellular pathogens</searchLink><br /><searchLink fieldCode="DE" term="%22Biomarkers%22">Biomarkers</searchLink><br /><searchLink fieldCode="DE" term="%22Mitochondria%22">Mitochondria</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Nosema+cuniculi%22">Nosema cuniculi</searchLink><br /><searchLink fieldCode="DE" term="%22Aerobic+bacteria%22">Aerobic bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Biosynthesis%22">Biosynthesis</searchLink><br /><searchLink fieldCode="DE" term="%22Sulfur+compounds%22">Sulfur compounds</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Microsporidia are highly specialized obligate intracellular parasites of other eukaryotes (including humans) that show extreme reduction at the molecular, cellular and biochemical level. Although microsporidia have long been considered as early branching eukaryotes that lack mitochondria, they have recently been shown to contain a tiny mitochondrial remnant called a mitosome. The function of the mitosome is unknown, because microsporidians lack the genes for canonical mitochondrial functions, such as aerobic respiration and haem biosynthesis. However, microsporidial genomes encode several components of the mitochondrial iron–sulphur (Fe–S) cluster assembly machinery. Here we provide experimental insights into the metabolic function and localization of these proteins. We cloned, functionally characterized and localized homologues of several central mitochondrial Fe–S cluster assembly components for the microsporidians Encephalitozoon cuniculi and Trachipleistophora hominis. Several microsporidial proteins can functionally replace their yeast counterparts in Fe–S protein biogenesis. In E. cuniculi, the iron (frataxin) and sulphur (cysteine desulphurase, Nfs1) donors and the scaffold protein (Isu1) co-localize with mitochondrial Hsp70 to the mitosome, consistent with it being the functional site for Fe–S cluster biosynthesis. In T. hominis, mitochondrial Hsp70 and the essential sulphur donor (Nfs1) are still in the mitosome, but surprisingly the main pools of Isu1 and frataxin are cytosolic, creating a conundrum of how these key components of Fe–S cluster biosynthesis coordinate their function. Together, our studies identify the essential biosynthetic process of Fe–S protein assembly as a key function of microsporidian mitosomes. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Nature is the property of Springer Nature 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=pbh&AN=31514383
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1038/nature06606
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 5
        StartPage: 624
    Subjects:
      – SubjectFull: Microsporidia
        Type: general
      – SubjectFull: Intracellular pathogens
        Type: general
      – SubjectFull: Biomarkers
        Type: general
      – SubjectFull: Mitochondria
        Type: general
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: Nosema cuniculi
        Type: general
      – SubjectFull: Aerobic bacteria
        Type: general
      – SubjectFull: Biosynthesis
        Type: general
      – SubjectFull: Sulfur compounds
        Type: general
    Titles:
      – TitleFull: Localization and functionality of microsporidian iron–sulphur cluster assembly proteins.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Goldberg, Alina V.
      – PersonEntity:
          Name:
            NameFull: Molik, Sabine
      – PersonEntity:
          Name:
            NameFull: Tsaousis, Anastasios D.
      – PersonEntity:
          Name:
            NameFull: Neumann, Karina
      – PersonEntity:
          Name:
            NameFull: Kuhnke, Grit
      – PersonEntity:
          Name:
            NameFull: Delbac, Frederic
      – PersonEntity:
          Name:
            NameFull: Vivares, Christian P.
      – PersonEntity:
          Name:
            NameFull: Hirt, Robert P.
      – PersonEntity:
          Name:
            NameFull: Lill, Roland
      – PersonEntity:
          Name:
            NameFull: Embley, T. Martin
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 03
              M: 04
              Text: 4/3/2008
              Type: published
              Y: 2008
          Identifiers:
            – Type: issn-print
              Value: 00280836
          Numbering:
            – Type: volume
              Value: 452
            – Type: issue
              Value: 7187
          Titles:
            – TitleFull: Nature
              Type: main
ResultId 1