Open Access

RNA Biology, volume 14, issue 6, pages 680-692

Assembly and trafficking of box C/D and H/ACA snoRNPs

Massenet Séverine ¹

Bertrand Edouard ²

Verheggen Céline ²

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Ingénierie Moléculaire et Physiopathologie Articulaire, UMR 7365 CNRS, 9 Avenue de la forêt de Haye, 54505 Vandoeuvre-les-Nancy Cedex, France, Université de Lorraine, Campus Biologie –Santé, CS 50184, 54505 Vandoeuvre-les-Nancy Cedex, France |

Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, 1919 route de Mende, 34293 Montpellier cedex 5, France, Université de Montpellier, 163 rue Auguste Broussonnet, 34090 Montpellier, France |

Publication type: Journal Article

Publication date: 2016-12-01

Taylor & Francis

Journal: RNA Biology

Quartile SCImago

Quartile WOS

Impact factor: 4.1

ISSN: 15476286, 15558584

DOI: 10.1080/15476286.2016.1243646

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PubMed ID: 27715451

Molecular Biology

Cell Biology

Abstract

ABSTRACT Box C/D and box H/ACA snoRNAs are abundant non-coding RNAs that localize in the nucleolus and mostly function as guides for nucleotide modifications. While a large pool of snoRNAs modifies rRNAs, an increasing number of snoRNAs could also potentially target mRNAs. ScaRNAs belong to a family of specific RNAs that localize in Cajal bodies and that are structurally similar to snoRNAs. Most scaRNAs are involved in snRNA modification, while telomerase RNA, which contains H/ACA motifs, functions in telomeric DNA synthesis. In this review, we describe how box C/D and H/ACA snoRNAs are processed and assembled with core proteins to form functional RNP particles. Their biogenesis involve several transport factors that first direct pre-snoRNPs to Cajal bodies, where some processing steps are believed to take place, and then to nucleoli. Assembly of core proteins involves the HSP90/R2TP chaperone-cochaperone system for both box C/D and H/ACA RNAs, but also several factors specific for each family. These assembly factors chaperone unassembled core proteins, regulate the formation and disassembly of pre-snoRNP intermediates, and control the activity of immature particles. The AAA+ ATPase RUVBL1 and RUVBL2 belong to the R2TP co-chaperones and play essential roles in snoRNP biogenesis, as well as in the formation of other macro-molecular complexes. Despite intensive research, their mechanisms of action are still incompletely understood.

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Journal of Biological Chemistry	Journal of Biological Chemistry, 2, 1.69% Journal of Biological Chemistry 2 publications, 1.69%
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Science advances	Science advances, 2, 1.69% Science advances 2 publications, 1.69%
Proceedings of the National Academy of Sciences of the United States of America	Proceedings of the National Academy of Sciences of the United States of America, 2, 1.69% Proceedings of the National Academy of Sciences of the United States of America 2 publications, 1.69%
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Frontiers in Microbiology	Frontiers in Microbiology, 1, 0.85% Frontiers in Microbiology 1 publication, 0.85%
Frontiers in Endocrinology	Frontiers in Endocrinology, 1, 0.85% Frontiers in Endocrinology 1 publication, 0.85%
Pathology and Oncology Research	Pathology and Oncology Research, 1, 0.85% Pathology and Oncology Research 1 publication, 0.85%
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Citations by publishers

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Public Library of Science (PLoS)	Public Library of Science (PLoS), 2, 1.69% Public Library of Science (PLoS) 2 publications, 1.69%
American Association for the Advancement of Science (AAAS)	American Association for the Advancement of Science (AAAS), 2, 1.69% American Association for the Advancement of Science (AAAS) 2 publications, 1.69%
Proceedings of the National Academy of Sciences (PNAS)	Proceedings of the National Academy of Sciences (PNAS), 2, 1.69% Proceedings of the National Academy of Sciences (PNAS) 2 publications, 1.69%
The Company of Biologists	The Company of Biologists, 1, 0.85% The Company of Biologists 1 publication, 0.85%
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American Physiological Society	American Physiological Society, 1, 0.85% American Physiological Society 1 publication, 0.85%
Annual Reviews	Annual Reviews, 1, 0.85% Annual Reviews 1 publication, 0.85%
American Society of Plant Biologists	American Society of Plant Biologists, 1, 0.85% American Society of Plant Biologists 1 publication, 0.85%
Mary Ann Liebert	Mary Ann Liebert, 1, 0.85% Mary Ann Liebert 1 publication, 0.85%
Portland Press	Portland Press, 1, 0.85% Portland Press 1 publication, 0.85%
	5 10 15 20 25

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Massenet S., Bertrand E., Verheggen C. Assembly and trafficking of box C/D and H/ACA snoRNPs // RNA Biology. 2016. Vol. 14. No. 6. pp. 680-692.

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Massenet S., Bertrand E., Verheggen C. Assembly and trafficking of box C/D and H/ACA snoRNPs // RNA Biology. 2016. Vol. 14. No. 6. pp. 680-692.

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RIS Copy

TY - JOUR

DO - 10.1080/15476286.2016.1243646

UR - https://doi.org/10.1080%2F15476286.2016.1243646

TI - Assembly and trafficking of box C/D and H/ACA snoRNPs

T2 - RNA Biology

AU - Massenet, Séverine

AU - Bertrand, Edouard

AU - Verheggen, Céline

PY - 2016

DA - 2016/12/01 00:00:00

PB - Taylor & Francis

SP - 680-692

IS - 6

VL - 14

PMID - 27715451

SN - 1547-6286

SN - 1555-8584

ER -

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@article{2016_Massenet,

author = {Séverine Massenet and Edouard Bertrand and Céline Verheggen},

title = {Assembly and trafficking of box C/D and H/ACA snoRNPs},

journal = {RNA Biology},

year = {2016},

volume = {14},

publisher = {Taylor & Francis},

month = {dec},

url = {https://doi.org/10.1080%2F15476286.2016.1243646},

number = {6},

pages = {680--692},

doi = {10.1080/15476286.2016.1243646}

}

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Massenet, Séverine, et al. “Assembly and trafficking of box C/D and H/ACA snoRNPs.” RNA Biology, vol. 14, no. 6, Dec. 2016, pp. 680-692. https://doi.org/10.1080%2F15476286.2016.1243646.

Found error?

Publisher

Taylor & Francis

Journal

RNA Biology

Quartile SCImago

Quartile WOS

Impact factor

4.1

ISSN

15476286 (Print)
15558584 (Electronic)