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PDBsum entry 2lo6
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Transcription
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PDB id
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2lo6
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References listed in PDB file
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Key reference
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Title
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Serine phosphorylation and proline isomerization in rnap ii ctd control recruitment of nrd1.
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Authors
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K.Kubicek,
H.Cerna,
P.Holub,
J.Pasulka,
D.Hrossova,
F.Loehr,
C.Hofr,
S.Vanacova,
R.Stefl.
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Ref.
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Genes Dev, 2012,
26,
1891-1896.
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PubMed id
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Abstract
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Recruitment of appropriate RNA processing factors to the site of transcription
is controlled by post-translational modifications of the C-terminal domain (CTD)
of RNA polymerase II (RNAP II). Here, we report the solution structure of the
Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct
recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream
pSer5-Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface
diminish binding affinity and impair processing or degradation of noncoding
RNAs. These findings underpin the interplay between covalent and noncovalent
changes in the CTD structure that constitute the CTD code.
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