IndraLab

Statements


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"The carboxy‐terminal region of the spliceosomal protein PRPF8, which modulates the RNA helicase Brr2, is a mutation hotspot linked to retinitis pigmentosa‐type 13, although its precise function in human splicing and tissue‐specific mechanisms remains unclear."

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"Although it has been demonstrated that the PRPF8 RNase H domain inhibits SNRNP200 activity and GTP bound EFTUD2 and that the C-terminus of PRPF8 induces the activation of SNRNP200 XREF_BIBR - XREF_BIBR, the detailed molecular mechanisms of the activation of SNRNP200 remains to be determined."

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"Prp8, which directly regulates Brr2 activity (Maeder et al. 2009; Nielsen and Staley 2012; Mozaffari-Jovin et al. 2013; Nguyen et al. 2013), has also been implicated in 3′SS selection (Umen and Guthrie 1995a,b, 1996; Siatecka et al. 1999) as well as the transition between the first and second catalytic steps (Frank et al. 1992; Query and Konarska 2004; Liu et al. 2007)."

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"Indeed a C-terminal fragment of Prp8 — encompassing the RNaseH-like and Jab/MPN1-like domains — strongly stimulates Brr2-dependent U4/U6 unwinding in vitro [ 44 ]."

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"The RNase H domain of PRPF8 inhibits loading of SNRNP200 to U4 snRNA, and a C-terminal part of PRPF8 modulates the SNRNP200 activity for the unwinding of U4/U6 snRNA duplex XREF_BIBR - XREF_BIBR."