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Lookup NU author(s): Dr Herve Chabanon, David Nury, Dr Ian Mickleburgh, Brian Burtle, Professor John Hesketh
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Subcellular localization of mRNAs is a key mechanism for the synthesis of proteins close to their site of function. The mRNA encoding MT-1 (metallothionein-1) is localized in the perinuclear cytoplasm, where it is associated with cytoskeletal-bound polysomes. This localization relies on sequences present in the 3′-UTR (3′-untranslated region). The present study aims to characterize the cis-acting localization element(s) within the 3′-UTR. Using transfected cells expressing tagged MT-1 differing in their 3′-UTRs (deleted or mutated), the section(s) of this region required for directing MT-1 transcripts to the perinuclear cytoplasm has been investigated. Different 3′-UTRs were also used in UV cross-linking experiments that highlighted two distinct regions (nt 26-30 and 66-76) necessary for the binding of a protein of approx. 50 kDa, presumably involved in the mRNA targeting. The poor sequence homology between the MT-1 3′-UTR of various species, together with the bipartite nature of the required cis-element, indicates the involvement of a particular structure in the localization signal. The secondary structure of the MT-1 3′-UTR was investigated using enzymic and chemical probing. Current structural analysis of mutant 3′-UTRs will allow the critical structural features of the MT-1 mRNA perinuclear localization signal to be defined.
Author(s): Chabanon H, Nury D, Mickleburgh I, Burtle B, Hesketh J
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: Bioscience 2004 Conference
Year of Conference: 2004
Pages: 702-704
ISSN: 0300-5127
Publisher: Biochemical Society Transactions: Portland Press
URL: http://dx.doi.org/10.1042/BST0320702
DOI: 10.1042/BST0320702
PubMed id: 15493992
