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Title: Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2

Abstract

Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97. Previous studies in Saccharomyces cerevisiae suggest that Rix7 mediates the release of Nsa1 from nucleolar pre-60S particles; however, the underlying mechanisms of this release are unknown. Through multiple structural analyses we show that S. cerevisiae Nsa1 is composed of an N-terminal seven-bladed WD40 domain followed by a lysine-rich C terminus that extends away from the WD40 domain and is required for nucleolar localization. Additional co-immunoprecipitation assays with the mammalian homologs identified a well-conserved interface within WDR74 that is important for its association with NVL2. We further show that WDR74 associates with the D1 AAA domain of NVL2, which represents a novel mode of binding of a substrate with a type II AAA-ATPase.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institute of Environmental Health Sciences (NIEHS); National Institutes of Health (NIHI)
OSTI Identifier:
1435653
Alternate Identifier(s):
OSTI ID: 1368256; OSTI ID: 1397654
Grant/Contract Number:  
W-31-109-Eng-38; AC02-05CH11231; ZIA ES103247; S10OD018483
Resource Type:
Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Name: Structure Journal Volume: 25 Journal Issue: 5; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United Kingdom
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; AAA-ATPase; ribosome assembly; WD40 domain; pre-rRNA processing

Citation Formats

Lo, Yu-Hua, Romes, Erin M., Pillon, Monica C., Sobhany, Mack, and Stanley, Robin E. Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2. United Kingdom: N. p., 2017. Web. doi:10.1016/j.str.2017.03.008.
Lo, Yu-Hua, Romes, Erin M., Pillon, Monica C., Sobhany, Mack, & Stanley, Robin E. Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2. United Kingdom. https://doi.org/10.1016/j.str.2017.03.008
Lo, Yu-Hua, Romes, Erin M., Pillon, Monica C., Sobhany, Mack, and Stanley, Robin E. Thu . "Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2". United Kingdom. https://doi.org/10.1016/j.str.2017.03.008.
@article{osti_1435653,
title = {Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2},
author = {Lo, Yu-Hua and Romes, Erin M. and Pillon, Monica C. and Sobhany, Mack and Stanley, Robin E.},
abstractNote = {Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97. Previous studies in Saccharomyces cerevisiae suggest that Rix7 mediates the release of Nsa1 from nucleolar pre-60S particles; however, the underlying mechanisms of this release are unknown. Through multiple structural analyses we show that S. cerevisiae Nsa1 is composed of an N-terminal seven-bladed WD40 domain followed by a lysine-rich C terminus that extends away from the WD40 domain and is required for nucleolar localization. Additional co-immunoprecipitation assays with the mammalian homologs identified a well-conserved interface within WDR74 that is important for its association with NVL2. We further show that WDR74 associates with the D1 AAA domain of NVL2, which represents a novel mode of binding of a substrate with a type II AAA-ATPase.},
doi = {10.1016/j.str.2017.03.008},
journal = {Structure},
number = 5,
volume = 25,
place = {United Kingdom},
year = {Thu Apr 13 00:00:00 EDT 2017},
month = {Thu Apr 13 00:00:00 EDT 2017}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1016/j.str.2017.03.008

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Cited by: 16 works
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