Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/13525
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
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 |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.