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  • Functional characterization of alternatively spliced human SECISBP2 transcript variants

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    Author(s)
    Papp, Laura V
    Wang, Junning
    Kennedy, Derek
    Boucher, Didier
    Zhang, Yan
    Gladyshev, Vadim N
    Singh, Ravindra N
    Khanna, Kum Kum
    Griffith University Author(s)
    Kennedy, Derek D.
    Year published
    2008
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    Abstract
    Synthesis of selenoproteins depends on decoding of the UGA stop codon as the amino acid selenocysteine (Sec). This process requires the presence of a Sec insertion sequence element (SECIS) in the 3'-untranslated region of selenoprotein mRNAs and its interaction with the SECIS binding protein 2 (SBP2). In humans, mutations in the SBP2-encoding gene Sec insertion sequence binding protein 2 (SECISBP2) that alter the amino acid sequence or cause splicing defects lead to abnormal thyroid hormone metabolism. Herein, we present the first in silico and in vivo functional characterization of alternative splicing of SECISBP2. We report ...
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    Synthesis of selenoproteins depends on decoding of the UGA stop codon as the amino acid selenocysteine (Sec). This process requires the presence of a Sec insertion sequence element (SECIS) in the 3'-untranslated region of selenoprotein mRNAs and its interaction with the SECIS binding protein 2 (SBP2). In humans, mutations in the SBP2-encoding gene Sec insertion sequence binding protein 2 (SECISBP2) that alter the amino acid sequence or cause splicing defects lead to abnormal thyroid hormone metabolism. Herein, we present the first in silico and in vivo functional characterization of alternative splicing of SECISBP2. We report a complex splicing pattern in the 5'-region of human SECISBP2, wherein at least eight splice variants encode five isoforms with varying N-terminal sequence. One of the isoforms, mtSBP2, contains a mitochondrial targeting sequence and localizes to mitochondria. Using a minigene-based in vivo splicing assay we characterized the splicing efficiency of several alternative transcripts, and show that the splicing event that creates mtSBP2 can be modulated by antisense oligonucleotides. Moreover, we show that full-length SBP2 and some alternatively spliced variants are subject to a coordinated transcriptional and translational regulation in response to ultraviolet type A irradiation-induced stress. Overall, our data broadens the functional scope of a housekeeping protein essential to selenium metabolism.
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    Journal Title
    Nucleic Acids Research
    Volume
    36
    Issue
    22
    DOI
    https://doi.org/10.1093/nar/gkn829
    Copyright Statement
    © 2008 The Author(s). This is an open access paper under the Creative Commons Attribution 3.0 Unported (CC BY 3.0) license that permits unrestricted use, provided that the paper is properly attributed.
    Subject
    Environmental sciences
    Biological sciences
    Biochemistry and cell biology not elsewhere classified
    Information and computing sciences
    Publication URI
    http://hdl.handle.net/10072/22519
    Collection
    • Journal articles

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