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Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis

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Title: Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis
Authors: Asano, Nozomi Browse this author
Kato, Koji Browse this author
Nakamura, Akiyoshi Browse this author
Komoda, Keisuke Browse this author
Tanaka, Isao Browse this author
Yao, Min Browse this author →KAKEN DB
Issue Date: 19-May-2015
Publisher: Oxford University Press
Journal Title: Nucleic acids research
Volume: 43
Issue: 9
Start Page: 4746
End Page: 4757
Publisher DOI: 10.1093/nar/gkv305
PMID: 25855814
Abstract: Proteins Rpf2 and Rrs1 are required for 60S ribosomal subunit maturation. These proteins are necessary for the recruitment of three ribosomal components (5S ribosomal RNA [rRNA], RpL5 and RpL11) to the 90S ribosome precursor and subsequent 27SB pre-rRNA processing. Here we present the crystal structure of the Aspergillus nidulans (An) Rpf2-Rrs1 core complex. The core complex contains the tightly interlocked N-terminal domains of Rpf2 and Rrs1. The Rpf2 N-terminal domain includes a Brix domain characterized by similar N-and C-terminal architecture. The long alpha-helix of Rrs1 joins the C-terminal half of the Brix domain as if it were part of a single molecule. The conserved proline-rich linker connecting the N- and C-terminal domains of Rrs1 wrap around the side of Rpf2 and anchor the C-terminal domain of Rrs1 to a specific site on Rpf2. In addition, gel shift analysis revealed that the Rpf2-Rrs1 complex binds directly to 5S rRNA. Further analysis of Rpf2-Rrs1 mutants demonstrated that Saccha-romyces cerevisiae Rpf2 R236 (corresponds to R238 of AnRpf2) plays a significant role in this binding. Based on these studies and previous reports, we have proposed a model for ribosomal component recruitment to the 90S ribosome precursor.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 姚 閔

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