The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly. / Aquino, Gerald Ryan R.; Hackert, Philipp; Krogh, Nicolai; Pan, Kuan Ting; Jaafar, Mariam; Henras, Anthony K.; Nielsen, Henrik; Urlaub, Henning; Bohnsack, Katherine E.; Bohnsack, Markus T.

I: Nature Communications, Bind 12, 6152, 2021.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Aquino, GRR, Hackert, P, Krogh, N, Pan, KT, Jaafar, M, Henras, AK, Nielsen, H, Urlaub, H, Bohnsack, KE & Bohnsack, MT 2021, 'The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly', Nature Communications, bind 12, 6152. https://doi.org/10.1038/s41467-021-26208-9

APA

Aquino, G. R. R., Hackert, P., Krogh, N., Pan, K. T., Jaafar, M., Henras, A. K., Nielsen, H., Urlaub, H., Bohnsack, K. E., & Bohnsack, M. T. (2021). The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly. Nature Communications, 12, [6152]. https://doi.org/10.1038/s41467-021-26208-9

Vancouver

Aquino GRR, Hackert P, Krogh N, Pan KT, Jaafar M, Henras AK o.a. The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly. Nature Communications. 2021;12. 6152. https://doi.org/10.1038/s41467-021-26208-9

Author

Aquino, Gerald Ryan R. ; Hackert, Philipp ; Krogh, Nicolai ; Pan, Kuan Ting ; Jaafar, Mariam ; Henras, Anthony K. ; Nielsen, Henrik ; Urlaub, Henning ; Bohnsack, Katherine E. ; Bohnsack, Markus T. / The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly. I: Nature Communications. 2021 ; Bind 12.

Bibtex

@article{f2ff5f0d3c5c4856a4de4979d96da80e,
title = "The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly",
abstract = "Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.",
author = "Aquino, {Gerald Ryan R.} and Philipp Hackert and Nicolai Krogh and Pan, {Kuan Ting} and Mariam Jaafar and Henras, {Anthony K.} and Henrik Nielsen and Henning Urlaub and Bohnsack, {Katherine E.} and Bohnsack, {Markus T.}",
note = "Publisher Copyright: {\textcopyright} 2021, The Author(s).",
year = "2021",
doi = "10.1038/s41467-021-26208-9",
language = "English",
volume = "12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

AU - Aquino, Gerald Ryan R.

AU - Hackert, Philipp

AU - Krogh, Nicolai

AU - Pan, Kuan Ting

AU - Jaafar, Mariam

AU - Henras, Anthony K.

AU - Nielsen, Henrik

AU - Urlaub, Henning

AU - Bohnsack, Katherine E.

AU - Bohnsack, Markus T.

N1 - Publisher Copyright: © 2021, The Author(s).

PY - 2021

Y1 - 2021

N2 - Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.

AB - Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.

U2 - 10.1038/s41467-021-26208-9

DO - 10.1038/s41467-021-26208-9

M3 - Journal article

C2 - 34686661

AN - SCOPUS:85117694360

VL - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 6152

ER -

ID: 284178522