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  Reverse genetic approaches in plants and yeast suggest a role for novel, evolutionarily conserved, selenoprotein-related genes in oxidative stress defense

Rodrigo, M. J., Moskovitz, J., Salamini, F., & Bartels, D. (2002). Reverse genetic approaches in plants and yeast suggest a role for novel, evolutionarily conserved, selenoprotein-related genes in oxidative stress defense. Molecular Genetics and Genomics, 267(5), 613-621.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3DBA-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3DBC-4
Genre: Journal Article

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 Creators:
Rodrigo, M. J., Author
Moskovitz, J., Author
Salamini, F.1, Author              
Bartels, D.1, Author              
Affiliations:
1Dept. of Plant Breeding and Yield Physiology (Francesco Salamini), MPI for Plant Breeding Research, Max Planck Society, ou_1113570              

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Free keywords: oxidative stress; PilB; selenoprotein; methionine sulfoxide reductase; reverse genetics
 Abstract: Oxidation of methionine residues during periods of oxidative stress can lead to loss of protein function. Organisms have developed defense strategies to minimize such damage. The PilB protein, which is involved in pilus formation in the pathogen Neisseria gonorrhoeae, is composed of three functional protein domains (I-III) with putative roles in oxidative stress defense. These domains are evolutionarily conserved and homologs have been discovered in diverse prokaryotes and eukaryotes. Domain III shows similarities to selenoproteins which contain selenium instead of sulfur in a conserved cysteine residue. The substitution of selenium for sulfur alters the redox properties of such proteins. Knock-out mutants were used to elucidate the function of these novel selenoprotein-like domains in yeast and in Arabidopsis thaliana. We show that organisms with non-functional genes for selenoprotein-like polypeptides accumulate higher levels of oxidized methionine residues on exposure to oxidative stress. The behavior of the mutants suggests that these novel selenoprotein-like gene products are part of a ubiquitous detoxification system that interacts with other redox-related proteins such as the thioredoxin-related protein and methionine sulfoxide reductase which are encoded by domains I and II of PilB. These proteins may be encoded by one gene as in the case of several prokaryotes, or by separate genes as in the eukaryotes examined here.

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Language(s): eng - English
 Dates: 2002-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 28787
ISI: 000177449600007
 Degree: -

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Title: Molecular Genetics and Genomics
  Alternative Title : Mol. Genet. Genomics
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 267 (5) Sequence Number: - Start / End Page: 613 - 621 Identifier: ISSN: 1617-4615