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The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome

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The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. / Gorna, M.; Pietras, Z.; Tsai, Y.; Callaghan, Anastasia; Hernandez, H.; Robinson, Carol V.; Luisi, B.

In: RNA, Vol. 16, No. 3, 2010, p. 553-562.

Research output: Contribution to journalArticle

Harvard

Gorna, M, Pietras, Z, Tsai, Y, Callaghan, A, Hernandez, H, Robinson, CV & Luisi, B 2010, 'The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome', RNA, vol. 16, no. 3, pp. 553-562. https://doi.org/10.1261/rna.1858010

APA

Gorna, M., Pietras, Z., Tsai, Y., Callaghan, A., Hernandez, H., Robinson, C. V., & Luisi, B. (2010). The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. RNA, 16(3), 553-562. https://doi.org/10.1261/rna.1858010

Vancouver

Author

Gorna, M. ; Pietras, Z. ; Tsai, Y. ; Callaghan, Anastasia ; Hernandez, H. ; Robinson, Carol V. ; Luisi, B. / The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. In: RNA. 2010 ; Vol. 16, No. 3. pp. 553-562.

Bibtex

@article{830b6d0e947a4b96af18fd9d2a87c84f,
title = "The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome",
abstract = "The Escherichia coli endoribonuclease RNase E is an essential enzyme having key roles in mRNA turnover and the processing of several structured RNA precursors, and it provides the scaffold to assemble the multienzyme RNA degradosome. The activity of RNase E is inhibited by the protein RraA, which can interact with the ribonuclease's degradosome-scaffolding domain. Here, we report that RraA can bind to the RNA helicase component of the degradosome (RhlB) and the two RNA-binding sites in the degradosome-scaffolding domain of RNase E. In the presence of ATP, the helicase can facilitate the exchange of RraA for RNA stably bound to the degradosome. Our data suggest that RraA can affect multiple components of the RNA degradosome in a dynamic, energy-dependent equilibrium. The multidentate interactions of RraA impede the RNA-binding and ribonuclease activities of the degradosome and may result in complex modulation and rerouting of degradosome activity.",
author = "M. Gorna and Z. Pietras and Y. Tsai and Anastasia Callaghan and H. Hernandez and Robinson, {Carol V.} and B. Luisi",
year = "2010",
doi = "10.1261/rna.1858010",
language = "English",
volume = "16",
pages = "553--562",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "3",

}

RIS

TY - JOUR

T1 - The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome

AU - Gorna, M.

AU - Pietras, Z.

AU - Tsai, Y.

AU - Callaghan, Anastasia

AU - Hernandez, H.

AU - Robinson, Carol V.

AU - Luisi, B.

PY - 2010

Y1 - 2010

N2 - The Escherichia coli endoribonuclease RNase E is an essential enzyme having key roles in mRNA turnover and the processing of several structured RNA precursors, and it provides the scaffold to assemble the multienzyme RNA degradosome. The activity of RNase E is inhibited by the protein RraA, which can interact with the ribonuclease's degradosome-scaffolding domain. Here, we report that RraA can bind to the RNA helicase component of the degradosome (RhlB) and the two RNA-binding sites in the degradosome-scaffolding domain of RNase E. In the presence of ATP, the helicase can facilitate the exchange of RraA for RNA stably bound to the degradosome. Our data suggest that RraA can affect multiple components of the RNA degradosome in a dynamic, energy-dependent equilibrium. The multidentate interactions of RraA impede the RNA-binding and ribonuclease activities of the degradosome and may result in complex modulation and rerouting of degradosome activity.

AB - The Escherichia coli endoribonuclease RNase E is an essential enzyme having key roles in mRNA turnover and the processing of several structured RNA precursors, and it provides the scaffold to assemble the multienzyme RNA degradosome. The activity of RNase E is inhibited by the protein RraA, which can interact with the ribonuclease's degradosome-scaffolding domain. Here, we report that RraA can bind to the RNA helicase component of the degradosome (RhlB) and the two RNA-binding sites in the degradosome-scaffolding domain of RNase E. In the presence of ATP, the helicase can facilitate the exchange of RraA for RNA stably bound to the degradosome. Our data suggest that RraA can affect multiple components of the RNA degradosome in a dynamic, energy-dependent equilibrium. The multidentate interactions of RraA impede the RNA-binding and ribonuclease activities of the degradosome and may result in complex modulation and rerouting of degradosome activity.

U2 - 10.1261/rna.1858010

DO - 10.1261/rna.1858010

M3 - Article

VL - 16

SP - 553

EP - 562

JO - RNA

JF - RNA

SN - 1355-8382

IS - 3

ER -

ID: 34739