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Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E

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Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E. / Callaghan, Anastasia; Aurikko, J.; Ilag, L.; Gunter Grossmann, J.; Chandran, V.; Kuhnel, K.; Poljak, L.; Carpousis, A.; Robinson, Carol V.; Symmons, M.; Luisi, B.

In: Journal of Molecular Biology, Vol. 340, No. 5, 2004, p. 965-979.

Research output: Contribution to journalArticle

Harvard

Callaghan, A, Aurikko, J, Ilag, L, Gunter Grossmann, J, Chandran, V, Kuhnel, K, Poljak, L, Carpousis, A, Robinson, CV, Symmons, M & Luisi, B 2004, 'Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E', Journal of Molecular Biology, vol. 340, no. 5, pp. 965-979. https://doi.org/10.1016/j.jmb.2004.05.046

APA

Callaghan, A., Aurikko, J., Ilag, L., Gunter Grossmann, J., Chandran, V., Kuhnel, K., ... Luisi, B. (2004). Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E. Journal of Molecular Biology, 340(5), 965-979. https://doi.org/10.1016/j.jmb.2004.05.046

Vancouver

Callaghan A, Aurikko J, Ilag L, Gunter Grossmann J, Chandran V, Kuhnel K et al. Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E. Journal of Molecular Biology. 2004;340(5):965-979. https://doi.org/10.1016/j.jmb.2004.05.046

Author

Callaghan, Anastasia ; Aurikko, J. ; Ilag, L. ; Gunter Grossmann, J. ; Chandran, V. ; Kuhnel, K. ; Poljak, L. ; Carpousis, A. ; Robinson, Carol V. ; Symmons, M. ; Luisi, B. / Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E. In: Journal of Molecular Biology. 2004 ; Vol. 340, No. 5. pp. 965-979.

Bibtex

@article{41facec1f18449b89d9d107ac3d3fddf,
title = "Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E",
abstract = "The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10–40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein–RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed.",
author = "Anastasia Callaghan and J. Aurikko and L. Ilag and {Gunter Grossmann}, J. and V. Chandran and K. Kuhnel and L. Poljak and A. Carpousis and Robinson, {Carol V.} and M. Symmons and B. Luisi",
year = "2004",
doi = "10.1016/j.jmb.2004.05.046",
language = "English",
volume = "340",
pages = "965--979",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Studies of the RNA degradosome-organizing domain of the Escherichia coli Ribonuclease RNase E

AU - Callaghan, Anastasia

AU - Aurikko, J.

AU - Ilag, L.

AU - Gunter Grossmann, J.

AU - Chandran, V.

AU - Kuhnel, K.

AU - Poljak, L.

AU - Carpousis, A.

AU - Robinson, Carol V.

AU - Symmons, M.

AU - Luisi, B.

PY - 2004

Y1 - 2004

N2 - The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10–40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein–RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed.

AB - The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10–40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein–RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed.

U2 - 10.1016/j.jmb.2004.05.046

DO - 10.1016/j.jmb.2004.05.046

M3 - Article

VL - 340

SP - 965

EP - 979

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 5

ER -

ID: 158502