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Title
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The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing.
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Authors
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R.N.Jackson,
A.A.Klauer,
B.J.Hintze,
H.Robinson,
A.van Hoof,
S.J.Johnson.
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Ref.
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Embo J, 2010,
29,
2205-2216.
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PubMed id
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Abstract
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The essential RNA helicase, Mtr4, performs a critical role in RNA processing and
degradation as an activator of the nuclear exosome. The molecular basis for this
vital function is not understood and detailed analysis is significantly limited
by the lack of structural data. In this study, we present the crystal structure
of Mtr4. The structure reveals a new arch-like domain that is specific to Mtr4
and Ski2 (the cytosolic homologue of Mtr4). In vivo and in vitro analyses
demonstrate that the Mtr4 arch domain is required for proper 5.8S rRNA
processing, and suggest that the arch functions independently of canonical
helicase activity. In addition, extensive conservation along the face of the
putative RNA exit site highlights a potential interface with the exosome. These
studies provide a molecular framework for understanding fundamental aspects of
helicase function in exosome activation, and more broadly define the molecular
architecture of Ski2-like helicases.
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