Linked Life Data

7496404

Source:http://linkedlifedata.com/resource/pubmed/id/7496404

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-1-16
pubmed:abstractText
ATHSF1 is a heat shock transcription factor (HSF) of Arabidopsis that is constitutively expressed but its activity for DNA binding, trimer formation and transcriptional activation of heat shock (hs) genes is repressed at normal temperatures. In this study the functional properties of chimeric HSF-glucuronidase (GUS) fusion proteins were tested. Ectopic expression of HSF-GUS or GUS-HSF in transgenic Arabidopsis plants resulted in a derepression of HSF functions as shown by trimer formation, specific DNA binding, and the constitutive expression of heat shock proteins (HSPs) at normal temperature. A novel GUS activity-staining protocol was used to show the specific binding of trimeric HSF fusion proteins to DNA and following hs, an interaction between chimeric HSF-GUS and authentic HSF proteins. The chimeric HSFs were insensitive to the negative regulation that counteracts activation of the authentic HSF at normal temperature. Heterotrimer complexes were reconstituted in vitro from recombinant ATHSF1 and HSF-GUS proteins expressed in Escherichia coli and using this protocol, the temperature-dependent activation of wt HSF was monitored in vivo and in vitro. Transgenic plants expressing constitutively active HSF-GUS fusion proteins are also constitutive for HSPs. Approximately 20% of the maximum heat-inducible levels of HSP18 were already present at normal temperature. The level of basic thermotolerance was significantly enhanced in these plants. The results indicate that genetic engineering using protein fusion is a very effective means to derepress the activity of an important regulatory protein in plants, that consequently activates a constitutive hs response in the absence of heat stress and eventually alters the thermotolerance phenotype.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
603-12
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7496404-Acclimatization, pubmed-meshheading:7496404-Agrobacterium tumefaciens, pubmed-meshheading:7496404-Arabidopsis, pubmed-meshheading:7496404-Arabidopsis Proteins, pubmed-meshheading:7496404-Blotting, Northern, pubmed-meshheading:7496404-Blotting, Western, pubmed-meshheading:7496404-Cloning, Molecular, pubmed-meshheading:7496404-DNA-Binding Proteins, pubmed-meshheading:7496404-Escherichia coli, pubmed-meshheading:7496404-Gene Expression Regulation, Plant, pubmed-meshheading:7496404-Genetic Engineering, pubmed-meshheading:7496404-Glucuronidase, pubmed-meshheading:7496404-Heat-Shock Proteins, pubmed-meshheading:7496404-Hot Temperature, pubmed-meshheading:7496404-Plant Proteins, pubmed-meshheading:7496404-Plants, Genetically Modified, pubmed-meshheading:7496404-RNA, Messenger, pubmed-meshheading:7496404-Recombinant Fusion Proteins, pubmed-meshheading:7496404-Transcription Factors, pubmed-meshheading:7496404-Transformation, Genetic
pubmed:year
1995
pubmed:articleTitle
Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis.
pubmed:affiliation
Lehrstuhl für Allgemeine Genetik, Universität Tübingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't