Institutions
|
About Us
|
Help
|
Gaeilge
0
1000
Home
Browse
Advanced Search
Search History
Marked List
Statistics
A
A
A
Author(s)
Institution
Publication types
Funder
Year
Limited By:
Subject = RNA-protein complexes;
1 items found
Sort by
Title
Author
Item type
Date
Institution
Peer review status
Language
Order
Ascending
Descending
25
50
100
per page
Bibtex
CSV
EndNote
RefWorks
RIS
XML
Displaying Results 1 - 1 of 1 on page 1 of 1
Marked
Mark
Multiple RNA structures affect translation initiation and UGA redefinition efficiency during synthesis of selenoprotein P
(2017)
Mariotti, Marco; Shetty, Sumangala; Baird, Lisa; Wu, Sen; Loughran, Gary; Copeland, Pau...
Multiple RNA structures affect translation initiation and UGA redefinition efficiency during synthesis of selenoprotein P
(2017)
Mariotti, Marco; Shetty, Sumangala; Baird, Lisa; Wu, Sen; Loughran, Gary; Copeland, Paul R.; Atkins, John F.; Howard, Michael T.
Abstract:
Gene-specific expansion of the genetic code allows for UGA codons to specify the amino acid selenocysteine (Sec). A striking example of UGA redefinition occurs during translation of the mRNA coding for the selenium transport protein, selenoprotein P (SELENOP), which in vertebrates may contain up to 22 in-frame UGA codons. Sec incorporation at the first and downstream UGA codons occurs with variable efficiencies to control synthesis of full-length and truncated SELENOP isoforms. To address how the Selenop mRNA can direct dynamic codon redefinition in different regions of the same mRNA, we undertook a comprehensive search for phylogenetically conserved RNA structures and examined the function of these structures using cell-based assays, in vitro translation systems, and in vivo ribosome profiling of liver tissue from mice carrying genomic deletions of 3′ UTR selenocysteine-insertion-sequences (SECIS1 and SECIS2). The data support a novel RNA structure near the start codon that impacts...
http://hdl.handle.net/10468/5387
Displaying Results 1 - 1 of 1 on page 1 of 1
Bibtex
CSV
EndNote
RefWorks
RIS
XML
built by Enovation Solutions