Linked Life Data

1450386

Source:http://linkedlifedata.com/resource/pubmed/id/1450386

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-1-7
pubmed:abstractText
A hammerhead ribozyme designed against the mRNA coding for the Escherichia coli beta-glucuronidase (GUS) reporter enzyme was constructed. The synthetic ribozyme appeared able to correctly cleave in vitro the target RNA. This catalytic molecule was then assayed for in vivo activity in plant protoplasts. Plasmids coding either for the ribozyme or for the GUS target gene were cotransfected into the cells by the PEG-calcium procedure and GUS gene expression monitored following transient expression by measuring the intracellular GUS enzymatic activity. Expression of the ribozyme to high molar excess over the GUS transcript did not lead to any significant decrease of GUS activity in the transfected protoplasts. Insertion of the ribozyme sequence in the 3'-untranslated region of the GUS mRNA also had no detectable effect on GUS reporter gene expression whereas the corresponding RNA appeared able to self-cleave in vitro. These results indicate that the ability of ribozymes to perform catalytic cleavage of their substrate mRNA in vitro is essential but clearly not sufficient to ensure that efficient inhibition of the corresponding target gene will occur upon endogenous expression of this catalytic RNA in the plant cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:geneSymbol
GUS
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
715-31
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Assaying synthetic ribozymes in plants: high-level expression of a functional hammerhead structure fails to inhibit target gene activity in transiently transformed protoplasts.
pubmed:affiliation
Laboratoire de Biologie Moléculaire des Relations Plantes-Microorganismes, CNRS-INRA (UMR CNRS), Castanet-Tolosan, France.
pubmed:publicationType
Journal Article