TY  - JOUR
A1  - Veith, Thomas
A1  - Martin, Roman
A1  - Wurm, Jan Philip
A1  - Weis, Benjamin L.
A1  - Duchardt-Ferner, Elke
A1  - Safferthal, Charlotta
A1  - Hennig, Raoul
A1  - Mirus, Oliver
A1  - Bohnsack, Markus
A1  - Wöhnert, Jens
A1  - Schleiff, Enrico
T1  - Structural and functional analysis of the archaeal endonuclease Nob1
T2  - Nucleic acids research
N2  - Eukaryotic ribosome biogenesis requires the concerted action of numerous ribosome assembly factors, for most of which structural and functional information is currently lacking. Nob1, which can be identified in eukaryotes and archaea, is required for the final maturation of the small subunit ribosomal RNA in yeast by catalyzing cleavage at site D after export of the preribosomal subunit into the cytoplasm. Here, we show that this also holds true for Nob1 from the archaeon Pyrococcus horikoshii, which efficiently cleaves RNA-substrates containing the D-site of the preribosomal RNA in a manganese-dependent manner. The structure of PhNob1 solved by nuclear magnetic resonance spectroscopy revealed a PIN domain common with many nucleases and a zinc ribbon domain, which are structurally connected by a flexible linker. We show that amino acid residues required for substrate binding reside in the PIN domain whereas the zinc ribbon domain alone is sufficient to bind helix 40 of the small subunit rRNA. This suggests that the zinc ribbon domain acts as an anchor point for the protein on the nascent subunit positioning it in the proximity of the cleavage site.
Y1  - 2011
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/23230
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-232305
UR  - http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3326319/
SN  - 1362-4962
SN  - 0305-1048
N1  - (c) The Author(s) 2011. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
VL  - 40
IS  - 7
SP  - 3259
EP  - 3274
PB  - Oxford Univ. Press
CY  - Oxford
ER  -