NDLI: Isolation and Characterization of a New Peroxiredoxin from Poplar Sieve Tubes That Uses Either Glutaredoxin or Thioredoxin as a Proton Donor1

Content Provider	PubMed Central
Author	Nicolas, Rouhier Eric, Gelhaye Sautiere, Pierre-eric Brun, Annick Laurent, Pascal Denis, Tagu Gerard, Joelle De, Faÿ Elisabeth Meyer, Yves Jacquot, Jean-pierre
Copyright Year	2001
Abstract	A sequence coding for a peroxiredoxin (Prx) was isolated from a xylem/phloem cDNA library from Populus trichocarpa and subsequently inserted into an expression plasmid yielding the construction pET-Prx. The recombinant protein was produced in Escherichia coli cells and purified to homogeneity with a high yield. The poplar Prx is composed of 162 residues, a property that makes it the shortest plant Prx sequence isolated so far. It was shown that the protein is monomeric and possesses two conserved cysteines (Cys). The Prx degrades hydrogen peroxide and alkyl hydroperoxides in the presence of an exogenous proton donor that can be either thioredoxin or glutaredoxin (Grx). Based on this finding, we propose that the poplar protein represents a new type of Prx that differs from the so-called 2-Cys and 1-Cys Prx, a suggestion supported by the existence of natural fusion sequences constituted of a Prx motif coupled to a Grx motif. The protein was shown to be highly expressed in sieve tubes where thioredoxin h and Grx are also major proteins.
Starting Page	1299
File Format	PDF
ISSN	15322548
e-ISSN	15322548
Journal	Plant Physiology
Issue Number	3
Volume Number	127
Language	English
Publisher	American Society of Plant Physiologists
Publisher Date	2001-11-01
Access Restriction	Open
Rights Holder	American Society of Plant Physiologists
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Physiology Plant Science

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