Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1998-11-5
|
| pubmed:databankReference | |
| pubmed:abstractText |
A clone encoding a putative soluble epoxide hydrolase (EH-1), an enzyme which converts epoxides to diols, was isolated by differential screening of a cDNA library prepared from tobacco mosaic virus (TMV)-infected tobacco leaves. To confirm that EH-1 encodes an epoxide hydrolase, the recombinant EH-1 protein produced in bacteria was shown to have high epoxide hydrolase activity in vitro. Infection of resistant but not susceptible tobacco cultivars induced the accumulation of EH-1 transcripts in both the inoculated and uninoculated, systemic leaves. EH-1 expression was also induced in the inoculated and systemic tissues of TMV-infected NahG plants, which are unable to accumulate salicylic acid (SA). However, EH-1 expression in the inoculated leaves of NahG plants was delayed, whilst in the systemic leaves the induction was both later and weaker, compared to that observed in wild-type plants. Furthermore, exogenously applied SA or its functional analog 2,6-dichloroisonicotinic acid (INA) caused a rapid and transient accumulation of EH-1 transcripts, whereas an inactive SA analog did not. Thus, the induction of EH-1 gene expression appears to be regulated by both SA-independent and SA-dependent pathways. Since EH-1 was expressed only in TMV-resistant tobacco after infection, and the encoded enzyme is thought to help metabolize toxic compounds, we propose that EH-1 may play a role in protection from oxidative damage associated with defense responses. It may also play a role in generating signals for activation of certain defense responses.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,6-dichloroisonicotinic acid,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Epoxide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Indoleacetic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Isonicotinic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salicylic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0960-7412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
15
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
647-56
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9778847-Amino Acid Sequence,
pubmed-meshheading:9778847-Base Sequence,
pubmed-meshheading:9778847-Cloning, Molecular,
pubmed-meshheading:9778847-DNA, Plant,
pubmed-meshheading:9778847-Enzyme Induction,
pubmed-meshheading:9778847-Epoxide Hydrolases,
pubmed-meshheading:9778847-Escherichia coli,
pubmed-meshheading:9778847-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9778847-Gene Expression Regulation, Plant,
pubmed-meshheading:9778847-Genes, Plant,
pubmed-meshheading:9778847-Indoleacetic Acids,
pubmed-meshheading:9778847-Isonicotinic Acids,
pubmed-meshheading:9778847-Molecular Sequence Data,
pubmed-meshheading:9778847-Multigene Family,
pubmed-meshheading:9778847-Plants, Toxic,
pubmed-meshheading:9778847-Recombinant Proteins,
pubmed-meshheading:9778847-Salicylic Acid,
pubmed-meshheading:9778847-Temperature,
pubmed-meshheading:9778847-Tobacco,
pubmed-meshheading:9778847-Tobacco Mosaic Virus,
pubmed-meshheading:9778847-Viral Proteins
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Characterization of a tobacco epoxide hydrolase gene induced during the resistance response to TMV.
|
| pubmed:affiliation |
Waksman Institute, Rutgers, State University of New Jersey, Piscataway 08855, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|