Mammalian gene PEG10 expresses two reading frames by high efficiency - 1 frameshifting in embryonic-associated tissues

Clark, Michael B., Jänicke, Martina, Gottesbühren, Undine, Kleffmann, Torsten, Legge, Michael, Poole, Elizabeth S. and Tate, Warren P. (2007) Mammalian gene PEG10 expresses two reading frames by high efficiency - 1 frameshifting in embryonic-associated tissues. Journal of Biological Chemistry, 282 52: 37359-37369. doi:10.1074/jbc.M705676200

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Author Clark, Michael B.
Jänicke, Martina
Gottesbühren, Undine
Kleffmann, Torsten
Legge, Michael
Poole, Elizabeth S.
Tate, Warren P.
Title Mammalian gene PEG10 expresses two reading frames by high efficiency - 1 frameshifting in embryonic-associated tissues
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2007-12-28
Sub-type Article (original research)
DOI 10.1074/jbc.M705676200
Open Access Status File (Publisher version)
Volume 282
Issue 52
Start page 37359
End page 37369
Total pages 11
Editor Herbert Tabor
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Subject 0601 Biochemistry and Cell Biology
0904 Chemical Engineering
Formatted abstract
Paternally expressed gene 10 (PEG10) is a mammalian gene that is essential for embryonic development in mice. The gene contains two overlapping open reading frames (ORF1 and ORF2) and is derived from a retroelement that acquired a cellular function. It is not known if both reading frames are required for PEG10 function. Synthesis of ORF2 would be possible only if programmed - 1 frameshifting occurred during ORF1 translation. In this study the frameshifting activity of PEG10 was analyzed in vivo, and a potential role for ORF2 was investigated. Phylogenetic analysis demonstrated that PEG10 is highly conserved in therian mammals, with all species retaining the elements necessary for frameshifting as well as functional motifs in each ORF. The frameshift site of PEG10 was highly active in cultured cells and produced the ORF1-2 protein. In mice, endogenous ORF1 and an ORF1-2 frameshift protein were detected in the developing placenta and amniotic membrane from 9.5 days post-coitus through to term with a very high frameshift efficiency (>60%). Mutagenesis of the active site motif of a putative protease within ORF2 showed that this enzyme is active and participates in post-translational processing of PEG10 ORF1-2. Both PEG10 proteins were also detected in first trimester human placenta. By contrast, neither protein expression nor frameshifting was detected in adult mouse tissues. These studies imply that the ORF1-2 protein, synthesized utilizing the most efficient - 1 frameshift mechanism yet documented in vivo, will have an essential function that is intrinsic to the importance of PEG10 in mammals.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Keyword Cellular function
Embryonic development
Gene expression
PEG10 gene
Frameshift mutation
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 28 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 24 Mar 2010, 14:08:57 EST by June Temby on behalf of Faculty of Science