Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-3-8
pubmed:abstractText
The largest group of plant thioredoxins (TRXs) consists of the so-called h-type; their great number raises questions about their specific or redundant roles in plant cells. Pisum sativum thioredoxin h1 (PsTRXh1) and Pisum sativum thioredoxin h2 (PsTRXh2) are both h-type TRXs from pea (Pisum sativum) previously identified and biochemically characterized. While both are involved in redox regulation and show a high-sequence identity (60%), they display different behavior during in vitro and in vivo assays. In this work, we show that these two proteins display different specificity in the capturing of protein targets in vitro, by the use of a new stringent method. PsTRXh2 interacted with classical antioxidant proteins, whereas PsTRXh1 showed a completely different pattern of targeted proteins, and was able to capture a transcription factor. We also showed that the two proteins display very different thermal and chemical stabilities. We suggest that the differences in thermal and chemical stability point to a distinct and characteristic pattern of protein specificity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1618-1328
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Elsevier GmbH. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
167
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
423-9
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Evidence of non-functional redundancy between two pea h-type thioredoxins by specificity and stability studies.
pubmed:affiliation
Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental Zaidin, CSIC 18008 Granada, Spain. traverso@isv.cnrs-gif.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't