Universitat de Lleida
    • English
    • català
    • español
  • English 
    • English
    • català
    • español
  • Login
Repositori Obert UdL
View Item 
  •   Home
  • Recerca
  • Ciències Mèdiques Bàsiques
  • Articles publicats (Ciències Mèdiques Bàsiques)
  • View Item
  •   Home
  • Recerca
  • Ciències Mèdiques Bàsiques
  • Articles publicats (Ciències Mèdiques Bàsiques)
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism

Thumbnail
View/Open
10456.pdf (630.6Kb)
Issue date
2006
Author
Barreto Parra, Lina Patricia
Garcera, Ana
Jansson, Kristina
Sunnerhagen, Per
Herrero Perpiñán, Enrique
Suggested citation
Barreto Parra, Lina Patricia; Garcera, Ana; Jansson, Kristina; Sunnerhagen, Per; Herrero Perpiñán, Enrique; . (2006) . A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism. Eukaryotic cell, 2006, vol. 5, núm. 10, p. 1748-1759. https://doi.org/10.1128/EC.00216-06.
Impact


Web of Science logo    citations in Web of Science

Scopus logo    citations in Scopus

Google Scholar logo  Google Scholar
Share
Export to Mendeley
Metadata
Show full item record
Abstract
Saccharomyces cerevisiae cells contain three omega-class glutathione transferases with glutaredoxin activity (Gto1, Gto2, and Gto3), in addition to two glutathione transferases (Gtt1 and Gtt2) not classifiable into standard classes. Gto1 is located at the peroxisomes, where it is targeted through a PTS1-type sequence, whereas Gto2 and Gto3 are in the cytosol. Among the GTO genes, GTO2 shows the strongest induction of expression by agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide or cadmium, in a manner that is dependent on transcriptional factors Yap1 and/or Msn2/4. Diamide and 1-chloro-2,4-dinitrobenzene (causing depletion of reduced glutathione) also induce expression of GTO1 over basal levels. Phenotypic analyses with single and multiple mutants in the S. cerevisiae glutathione transferase genes show that, in the absence of Gto1 and the two Gtt proteins, cells display increased sensitivity to cadmium. A gto1-null mutant also shows growth defects on oleic acid-based medium, which is indicative of abnormal peroxisomal functions, and altered expression of genes related to sulfur amino acid metabolism. As a consequence, growth of the gto1 mutant is delayed in growth medium without lysine, serine, or threonine, and the mutant cells have low levels of reduced glutathione. The role of Gto1 at the S. cerevisiae peroxisomes could be related to the redox regulation of the Str3 cystathionine -lyase protein. This protein is also located at the peroxisomes in S. cerevisiae, where it is involved in transulfuration of cysteine into homocysteine, and requires a conserved cysteine residue for its biological activity.
URI
http://hdl.handle.net/10459.1/47217
DOI
https://doi.org/10.1128/EC.00216-06
Is part of
Eukaryotic cell, 2006, vol. 5, núm. 10, p. 1748-1759
European research projects
Collections
  • Articles publicats (Ciències Mèdiques Bàsiques) [580]
  • Articles publicats (IRBLleida) [1161]

Contact Us | Send Feedback | Legal Notice
© 2023 BiD. Universitat de Lleida
Metadata subjected to 
 

 

Browse

All of the repositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

Statistics

View Usage Statistics

D'interès

Política institucional d'accés obertDiposita les teves publicacionsDiposita dades de recercaSuport a la recerca

Contact Us | Send Feedback | Legal Notice
© 2023 BiD. Universitat de Lleida
Metadata subjected to