Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/13396
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Type: Journal article
Title: Cloning and expression of a distinct subclass of plant thioredoxins
Author: Juttner, J.
Olde, D.
Langridge, P.
Baumann, U.
Citation: FEBS Journal, 2000; 267(24):7109-7117
Publisher: Blackwell Publishing Ltd
Issue Date: 2000
ISSN: 1742-464X
0014-2956
Abstract: mRNAs encoding a novel thioredoxin were isolated from pollen RNA of Lolium perenne (LpTrx), Hordeum bulbosum (HbTrx), Phalaris coerulescens (PTrx) and Secale cereale (ScTrx). The cDNAs contain a single ORF of 393 bp encoding a protein of 131 amino acids. The predicted proteins showed highest homology to plant thioredoxins of the h class yet form a distinct subgroup that is characterized by a high level of sequence conservation (95.4-97.7% identity). GenBank searches revealed additional members of this subclass in tomato, soybean, rice and pine. LpTrx and PTrx were expressed as recombinant proteins in Escherichia coli and tested for thioredoxin activity. Both proteins displayed typical thioredoxin activity in the nonspecific insulin reduction assay, however, were not reduced by E. coli NADPH-dependant thioredoxin reductase.
Keywords: Lolium; Recombinant Proteins; DNA, Complementary; RNA, Messenger; Cloning, Molecular; Reverse Transcriptase Polymerase Chain Reaction; Amino Acid Sequence; Base Sequence; Sequence Homology, Amino Acid; Open Reading Frames; Molecular Sequence Data; Thioredoxins
RMID: 0001000414
DOI: 10.1046/j.1432-1327.2000.01811.x
Appears in Collections:Agriculture, Food and Wine publications

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