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Xp54 and related (DDX6-like) RNA helicases : roles in messenger RNP assembly, translation regulation and RNA degradation

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Date
07/2006
Author
Weston, A
Sommerville, John
Keywords
DEAD-BOX PROTEIN
PHYSIOLOGICAL GERMLINE APOPTOSIS
CYTOPLASMIC PROCESSING BODIES
STORED MRNP PARTICLES
Y-BOX
SACCHAROMYCES-CEREVISIAE
XENOPUS-OOCYTES
TRANSCRIPTION FACTOR
DNA-DAMAGE
RCK/P54
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Abstract
The DEAD-box RNA helicase Xp54 is an integral component of the messenger ribonucleoprotein (mRNP) particles of Xenopus oocytes. In oocytes, several abundant proteins bind pre-mRNA transcripts to modulate nuclear export, RNA stability and translational fate. Of these, Xp54, the mRNA-masking protein FRGY2 and its activating protein kinase CK2 alpha, bind to nascent transcripts on chromosome loops, whereas an Xp54-associated factor, RapA/B, binds to the mRNP complex in the cytoplasm. Over-expression, mutation and knockdown experiments indicate that Xp54 functions to change the conformation of mRNP complexes, displacing one subset of proteins to accommodate another. The sequence of Xp54 is highly conserved in a wide spectrum of organisms. Like Xp54, Drosophila Me31B and Caenorhabditis CGH-1 are required for proper meiotic development, apparently by regulating the translational activation of stored mRNPs and also for sorting certain mRNPs into germ plasm-containing structures. Studies on yeast Dhh1 and mammalian rck/p54 have revealed a key role for these helicases in mRNA degradation and in earlier remodelling of mRNP for entry into translation, storage or decay pathways. The versatility of Xp54 and related helicases in modulating the metabolism of mRNAs at all stages of their lifetimes marks them out as key regulators of post-transcriptional gene expression.
Citation
Weston , A & Sommerville , J 2006 , ' Xp54 and related (DDX6-like) RNA helicases : roles in messenger RNP assembly, translation regulation and RNA degradation ' , Nucleic Acids Research , vol. 34 , no. 10 , pp. 3082-3094 . https://doi.org/10.1093/nar/gkl409
Publication
Nucleic Acids Research
Status
Peer reviewed
DOI
https://doi.org/10.1093/nar/gkl409
ISSN
0305-1048
Type
Journal article
Rights
© 2006 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/4273

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