Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-8-10
pubmed:abstractText
The insulin-like growth factor II mRNAs are targets for site-specific endonucleolytic cleavage in the 3'-UTR, which results in a very stable 3' cleavage product of 1.8 kb, consisting of 3'-UTR sequences and a poly(A) tail. The 5' cleavage product contains the coding region and is rapidly degraded. Thus, cleavage is thought to provide an additional way to control IGF-II protein synthesis. We had established that cleavage requires two widely separated sequence elements (I and II) in the 3'-UTR that form a stable duplex of 83 nucleotides. The cleavage-site itself is located in an internal loop preceded by two stable stem-loop structures. Furthermore, in a study which was based on RNA folding algorithms, we have shown that there are specific sequence and structural requirements for the cleavage reaction. Here, the functions of the different structural domains in cleavage were assessed by deletion/mutational analyses, and biochemical structure probing assays were performed to characterize better the RNA structures formed and to verify the computer folding predictions. The data suggest that the stem-loop domain contributes to maintain a highly specific c leavage-site by preventing the formation of alternative structures in the cleavage-site domain. Involvement of the nucleotides in the cleavage-site loop itself in non-Watson-Crick interactions may be important for providing a specific recognition surface for an endoribonuclease activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
449-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10884343-3' Untranslated Regions, pubmed-meshheading:10884343-Base Pairing, pubmed-meshheading:10884343-Base Sequence, pubmed-meshheading:10884343-Cell Line, pubmed-meshheading:10884343-Computer Simulation, pubmed-meshheading:10884343-Humans, pubmed-meshheading:10884343-Insulin-Like Growth Factor II, pubmed-meshheading:10884343-Models, Genetic, pubmed-meshheading:10884343-Molecular Sequence Data, pubmed-meshheading:10884343-Nucleic Acid Conformation, pubmed-meshheading:10884343-RNA Processing, Post-Transcriptional, pubmed-meshheading:10884343-RNA Stability, pubmed-meshheading:10884343-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:10884343-Ribonucleases, pubmed-meshheading:10884343-Sequence Deletion, pubmed-meshheading:10884343-Structure-Activity Relationship, pubmed-meshheading:10884343-Substrate Specificity, pubmed-meshheading:10884343-Transfection
pubmed:year
2000
pubmed:articleTitle
Distinct RNA structural domains cooperate to maintain a specific cleavage site in the 3'-UTR of IGF-II mRNAs.
pubmed:affiliation
University Medical Center Utrecht, Department Physiological Chemistry, Utrecht, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't