Linked Life Data

8386879

Source:http://linkedlifedata.com/resource/pubmed/id/8386879

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-5-27
pubmed:abstractText
Initiation of protein synthesis on the foot-and-mouth disease virus RNA occurs at two sites, thus, two forms of the leader protein, termed Lab and Lb, are produced. Plasmids have been constructed which encode these proteins either together or individually. Plasmids encoding the Lab protein alone express a modified form of this protein in which the second methionine residue, which corresponds to the first amino acid of Lb, is changed to an alternative residue. Four different mutant forms of the Lab sequence were made. Each of the plasmids was introduced into a mammalian cell transient expression system which allowed the determination of the known activities of the L proteins. It was shown that the Lb protein and each of the modified Lab proteins were capable of cleaving the L/P1 junction in trans. Furthermore, each of these proteins induced the cleavage of the p220 component of the cap-binding complex (eIF-4F) producing inhibition of cap-dependent translation. These results indicate that the two species of L have the same functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
355-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities.
pubmed:affiliation
AFRC Institute for Animal Health, Pirbright, Woking, Surrey, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't