Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control

Autor: Christophe Charron, Xavier Manival, Céline Verheggen, Belinda J. Westman, Marie Eve Chagot, Heinrich Leonhardt, Angus I. Lamond, Séverine Boulon, Yasmeen Ahmad, Marie Hallais, Christiane Branlant, Jonathan Bizarro, Bérengère Pradet-Balade, Edouard Bertrand, Bruno Charpentier, Franck Vandermoere
Přispěvatelé: Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Ingénierie Moléculaire et Physiopathologie Articulaire ( IMoPA ), Université de Lorraine ( UL ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de recherches de biochimie macromoléculaire ( CRBM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Montpellier 2 - Sciences et Techniques ( UM2 ) -Université Montpellier 1 ( UM1 ), University of Dundee, Institut de Génomique Fonctionnelle - Montpellier GenomiX ( IGF MGX ), BioCenter and Center for Integrated Protein Science (CIPS), Ludwig-Maximilians-Universität München, Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Ludwig-Maximilians-Universität München (LMU)
Jazyk: angličtina
Rok vydání: 2014
Předmět:
Proteomics
Kruppel-Like Transcription Factors
RNA-binding protein
Plasma protein binding
Saccharomyces cerevisiae
Biology
Crystallography
X-Ray
Article
Ribonucleases
[ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Ribonucleoproteins
Small Nucleolar
Stable isotope labeling by amino acids in cell culture
Cell Line
Tumor
Proto-Oncogene Proteins
[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathology
Kruppel-Like Factor 6
Humans
Amino Acid Sequence
HSP90 Heat-Shock Proteins
Small nucleolar RNA
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Peptide sequence
Research Articles
R2TP complex
Ribonucleoprotein
Binding Sites
DNA Helicases
Nuclear Proteins
RNA-Binding Proteins
Cell Biology
Ribonucleoproteins
Small Nuclear
Molecular biology
AAA proteins
Cell biology
Neoplasm Proteins
DNA-Binding Proteins
HEK293 Cells
ATPases Associated with Diverse Cellular Activities
Carrier Proteins
Hydrophobic and Hydrophilic Interactions
Sequence Alignment
[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
HeLa Cells
Protein Binding
Transcription Factors
Zdroj: Journal of Cell Biology
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. 〈10.1083/jcb.201404160〉
Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.463-480. ⟨10.1083/jcb.201404160⟩
The Journal of Cell Biology
ISSN: 0021-9525
1540-8140
DOI: 10.1083/jcb.201404160〉
Popis: During small nucleolar ribonucleoprotein complex assembly, a pre-snoRNP complex consisting only of protein components forms first, followed by displacement of the ZNHIT3 subunit when C/D snoRNAs bind and dynamic loading and unloading of RuvBL AAA+ ATPases.
In vitro, assembly of box C/D small nucleolar ribonucleoproteins (snoRNPs) involves the sequential recruitment of core proteins to snoRNAs. In vivo, however, assembly factors are required (NUFIP, BCD1, and the HSP90–R2TP complex), and it is unknown whether a similar sequential scheme applies. In this paper, we describe systematic quantitative stable isotope labeling by amino acids in cell culture proteomic experiments and the crystal structure of the core protein Snu13p/15.5K bound to a fragment of the assembly factor Rsa1p/NUFIP. This revealed several unexpected features: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two core proteins, 15.5K and Nop58; (b) the characterization of ZNHIT3, which is present in the protein-only complex but gets released upon binding to C/D snoRNAs; (c) the dynamics of the R2TP complex, which appears to load/unload RuvBL AAA+ adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing premature activation of snoRNP catalytic activity. These data provide a framework for understanding the assembly of box C/D snoRNPs.
Databáze: OpenAIRE
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