 |
PDBsum entry 5by8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Biosynthetic protein
|
PDB id
|
|
|
|
5by8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structure of rpf2-Rrs1 explains its role in ribosome biogenesis.
|
|
|
Authors
|
|
S.Kharde,
F.R.Calviño,
A.Gumiero,
K.Wild,
I.Sinning.
|
|
|
Ref.
|
|
Nucleic Acids Res, 2015,
43,
7083-7095.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The assembly of eukaryotic ribosomes is a hierarchical process involving about
200 biogenesis factors and a series of remodeling steps. The 5S RNP consisting
of the 5S rRNA, RpL5 and RpL11 is recruited at an early stage, but has to
rearrange during maturation of the pre-60S ribosomal subunit. Rpf2 and Rrs1 have
been implicated in 5S RNP biogenesis, but their precise role was unclear. Here,
we present the crystal structure of the Rpf2-Rrs1 complex from Aspergillus
nidulans at 1.5 Å resolution and describe it as Brix domain of Rpf2 completed
by Rrs1 to form two anticodon-binding domains with functionally important tails.
Fitting the X-ray structure into the cryo-EM density of a previously described
pre-60S particle correlates with biochemical data. The heterodimer forms
specific contacts with the 5S rRNA, RpL5 and the biogenesis factor Rsa4. The
flexible protein tails of Rpf2-Rrs1 localize to the central protuberance. Two
helices in the Rrs1 C-terminal tail occupy a strategic position to block the
rotation of 25S rRNA and the 5S RNP. Our data provide a structural model for 5S
RNP recruitment to the pre-60S particle and explain why removal of Rpf2-Rrs1 is
necessary for rearrangements to drive 60S maturation.
|
|
|
|
|
|
|
