Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-8-5
pubmed:databankReference
pubmed:abstractText
Numerous studies argue that salicylic acid (SA) is an important component of the plant signal transduction pathway(s) leading to disease resistance. The discovery that the SA-binding protein is a catalase, whose activity is blocked by SA, led to the proposal that one of SA's modes of action is to inhibit this H2O2-degrading enzyme and thus elevate H2O2 levels. To test this model, an attempt was made to mimic the action of SA by reducing the synthesis of catalase using antisense RNA technology. Analyses of transgenic tobacco plants that expressed the tobacco catalase 1 (cat1) or catalase 2 (cat2) gene in an antisense orientation indicate that there is no correlation between modest to high levels of reduction in catalase activity and activation of plant defenses such as pathogenesis-related (PR)-1 protein synthesis. However, three independent antisense catalase transgenic plants (ASCAT1 Nos 16, 17, and 28), which exhibited the most severe reduction in catalase activity (approximately 90% or more), developed chlorosis or necrosis on some of their lower leaves. These same leaves accumulated very high levels of PR-1 proteins and showed enhanced resistance to tobacco mosaic virus. Necrosis and elevated SA, which appear to result from severe depression of catalase levels, may be responsible for the induction of these defense responses.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
993-1005
pubmed:dateRevised
2011-1-2
pubmed:meshHeading
pubmed-meshheading:9193071-Amino Acid Sequence, pubmed-meshheading:9193071-Base Sequence, pubmed-meshheading:9193071-Catalase, pubmed-meshheading:9193071-DNA, Antisense, pubmed-meshheading:9193071-DNA, Complementary, pubmed-meshheading:9193071-Escherichia coli, pubmed-meshheading:9193071-Gene Expression, pubmed-meshheading:9193071-Glucosides, pubmed-meshheading:9193071-Molecular Sequence Data, pubmed-meshheading:9193071-Necrosis, pubmed-meshheading:9193071-Plant Diseases, pubmed-meshheading:9193071-Plant Leaves, pubmed-meshheading:9193071-Plant Proteins, pubmed-meshheading:9193071-Plants, Genetically Modified, pubmed-meshheading:9193071-Plants, Toxic, pubmed-meshheading:9193071-Recombinant Proteins, pubmed-meshheading:9193071-Salicylic Acid, pubmed-meshheading:9193071-Salicylic Acids, pubmed-meshheading:9193071-Tobacco, pubmed-meshheading:9193071-Tobacco Mosaic Virus
pubmed:year
1997
pubmed:articleTitle
Development of necrosis and activation of disease resistance in transgenic tobacco plants with severely reduced catalase levels.
pubmed:affiliation
Department of Molecular Biology and Biochemistry, Rutgers, State University of New Jersey, Piscataway 08855-0759, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.