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  Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.

Rothé, B., Saliou, J. M., Quinternet, M., Back, R., Tiotiu, D., Jacquemin, C., et al. (2014). Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction. Nucleic Acids Research, 42(16), 10731-10747. doi:10.1093/nar/gku612.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-4576-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CC1B-E
Genre: Journal Article

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Rothé, B., Author
Saliou, J. M., Author
Quinternet, M., Author
Back, R., Author
Tiotiu, D., Author
Jacquemin, C., Author
Loegler, C., Author
Schlotter, F., Author
Pena, V.1, Author              
Eckert, K., Author
Moréra, S., Author
Dorsselaer, A. V., Author
Branlant, C., Author
Massenet, S., Author
Sanglier-Cianférani, S., Author
Manival, X., Author
Charpentier, B., Author
Affiliations:
1Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society, ou_2035293              

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 Abstract: Biogenesis of eukaryotic box C/D small nucleolar ribonucleoprotein particles (C/D snoRNPs) involves conservedtrans-acting factors, which are proposed to facilitate the assembly of the core proteins Snu13p/15.5K, Nop58p/NOP58, Nop56p/NOP56 and Nop1p/Fibrillarin on box C/D small nucleolar RNAs (C/D snoRNAs). In yeast, protein Rsa1 acts as a platform, interacting with both the RNA-binding core protein Snu13 and protein Pih1 of the Hsp82-R2TP chaperone complex. In this work, a proteomic approach coupled with functional and structural studies identifies protein Hit1 as a novel Rsa1p-interacting partner involved in C/D snoRNP assembly. Hit1p contributes to in vivo C/D snoRNA stability and pre-RNA maturation kinetics. It associates with U3 snoRNA precursors and influences its 3'-end processing. Remarkably, Hit1p is required to maintain steady-state levels of Rsa1p. This stabilizing activity is likely to be general across eukaryotic species, as the human protein ZNHIT3(TRIP3) showing sequence homology with Hit1p regulates the abundance of NUFIP1, the Rsa1p functional homolog. The nuclear magnetic resonance solution structure of the Rsa1p(317-352)-Hit1p(70-164) complex reveals a novel mode of protein-protein association explaining the strong stability of the Rsa1p-Hit1p complex. Our biochemical data show that C/D snoRNAs and the core protein Nop58 can interact with the purified Snu13p-Rsa1p-Hit1p heterotrimer.

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Language(s): eng - English
 Dates: 2014-08-282014-09-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gku612
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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 42 (16) Sequence Number: - Start / End Page: 10731 - 10747 Identifier: -