Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/13525
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Type: Journal article
Title: Thioredoxin activity in the C terminus of Phalaris S protein
Author: Li, Xinmin
Nield, Jan
Hayman, David
Langridge, Peter
Citation: Plant Journal,1995; 8(1):133-138
Publisher: Blackwell
Issue Date: 1995
ISSN: 0960-7412
Statement of
Responsibility: 
Xinmin Li, Jan Nield, David Hayman and Peter Langridge
Abstract: Self-incompatibility in the grass Phalaris coerulescens is controlled by two genes S and Z. Isolation and sequencing of two S alleles showed that they encode proteins that are highly conserved at the C terminus with significant homology to thioredoxin H proteins. In particular, the residues in and around the active site of thioredoxin, Trp-Cys-Gly-Pro-Cys, are perfectly conserved. The C terminus of the S protein has been expressed in Eschericia coli and purified to homogeneity on Ni-NTA resin. Functional assays showed that the protein has thioredoxin activity; it can act as a substrate for E. coli thioredoxin reductase and also catalyse the reduction of insulin by dithiothreitol. The possible role of thioredoxin-like activity of the S protein in mediating the incompatibility reaction in Phalaris is discussed.
Rights: © Unknown
DOI: 10.1046/j.1365-313X.1995.08010133.x
Appears in Collections:Agriculture, Food and Wine publications

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