Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli

Holger Lüttgen; Rudolf Robelek; René Mühlberger; Tammo Diercks; Stephan C. Schuster; Peter Köhler; Horst Kessler; Adelbert Bacher; Gerald Richter

doi:10.1006/jmbi.2001.5388

Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli

Holger Lüttgen, Rudolf Robelek, René Mühlberger, Tammo Diercks, Stephan C. Schuster, Peter Köhler, Horst Kessler, Adelbert Bacher, Gerald Richter

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Abstract

A recombinant heterodimeric NusB/NusE protein complex of Escherichia coli was expressed under the control of a synthetic mini operon. Surface plasmon resonance measurements showed that the heterodimer complex has substantially higher affinity for the boxA RNA sequence motif of the ribosomal RNA (rrn) operons of E. coli as compared to monomeric NusB protein. Single base exchanges in boxA RNA reduced the affinity of the protein complex up to 15-fold. The impact of base exchanges in the boxA RNA on the interaction with NusB protein was studied by ¹H,¹⁵N hetero-correlation NMR spectroscopy. Spectra obtained with modified RNA sequences were analysed by a novel generic algorithm. Replacement of bases in the terminal segments of the boxA RNA motif caused minor chemical shift changes as compared to base exchanges in the central part of the dodecameric boxA motif.

Originalsprache	Englisch
Seiten (von - bis)	875-885
Seitenumfang	11
Fachzeitschrift	Journal of Molecular Biology
Jahrgang	316
Ausgabenummer	4
DOIs	https://doi.org/10.1006/jmbi.2001.5388
Publikationsstatus	Veröffentlicht - 2002

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title = "Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli",

abstract = "A recombinant heterodimeric NusB/NusE protein complex of Escherichia coli was expressed under the control of a synthetic mini operon. Surface plasmon resonance measurements showed that the heterodimer complex has substantially higher affinity for the boxA RNA sequence motif of the ribosomal RNA (rrn) operons of E. coli as compared to monomeric NusB protein. Single base exchanges in boxA RNA reduced the affinity of the protein complex up to 15-fold. The impact of base exchanges in the boxA RNA on the interaction with NusB protein was studied by 1H,15N hetero-correlation NMR spectroscopy. Spectra obtained with modified RNA sequences were analysed by a novel generic algorithm. Replacement of bases in the terminal segments of the boxA RNA motif caused minor chemical shift changes as compared to base exchanges in the central part of the dodecameric boxA motif.",

keywords = "Antitermination, NMR spectroscopy, Protein/RNA interaction, Ribosomal RNA, Surface plasmon spectroscopy",

author = "Holger L{\"u}ttgen and Rudolf Robelek and Ren{\'e} M{\"u}hlberger and Tammo Diercks and Schuster, {Stephan C.} and Peter K{\"o}hler and Horst Kessler and Adelbert Bacher and Gerald Richter",

note = "Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft, the Volkswagen Stiftung and the Fonds der chemischen Industrie. We thank Professor D. Oesterhelt for advice and support.",

year = "2002",

doi = "10.1006/jmbi.2001.5388",

language = "English",

volume = "316",

pages = "875--885",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "4",

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TY - JOUR

T1 - Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli

AU - Lüttgen, Holger

AU - Robelek, Rudolf

AU - Mühlberger, René

AU - Diercks, Tammo

AU - Schuster, Stephan C.

AU - Köhler, Peter

AU - Kessler, Horst

AU - Bacher, Adelbert

AU - Richter, Gerald

N1 - Funding Information: This work was supported by grants from the Deutsche Forschungsgemeinschaft, the Volkswagen Stiftung and the Fonds der chemischen Industrie. We thank Professor D. Oesterhelt for advice and support.

PY - 2002

Y1 - 2002

N2 - A recombinant heterodimeric NusB/NusE protein complex of Escherichia coli was expressed under the control of a synthetic mini operon. Surface plasmon resonance measurements showed that the heterodimer complex has substantially higher affinity for the boxA RNA sequence motif of the ribosomal RNA (rrn) operons of E. coli as compared to monomeric NusB protein. Single base exchanges in boxA RNA reduced the affinity of the protein complex up to 15-fold. The impact of base exchanges in the boxA RNA on the interaction with NusB protein was studied by 1H,15N hetero-correlation NMR spectroscopy. Spectra obtained with modified RNA sequences were analysed by a novel generic algorithm. Replacement of bases in the terminal segments of the boxA RNA motif caused minor chemical shift changes as compared to base exchanges in the central part of the dodecameric boxA motif.

AB - A recombinant heterodimeric NusB/NusE protein complex of Escherichia coli was expressed under the control of a synthetic mini operon. Surface plasmon resonance measurements showed that the heterodimer complex has substantially higher affinity for the boxA RNA sequence motif of the ribosomal RNA (rrn) operons of E. coli as compared to monomeric NusB protein. Single base exchanges in boxA RNA reduced the affinity of the protein complex up to 15-fold. The impact of base exchanges in the boxA RNA on the interaction with NusB protein was studied by 1H,15N hetero-correlation NMR spectroscopy. Spectra obtained with modified RNA sequences were analysed by a novel generic algorithm. Replacement of bases in the terminal segments of the boxA RNA motif caused minor chemical shift changes as compared to base exchanges in the central part of the dodecameric boxA motif.

KW - Antitermination

KW - NMR spectroscopy

KW - Protein/RNA interaction

KW - Ribosomal RNA

KW - Surface plasmon spectroscopy

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U2 - 10.1006/jmbi.2001.5388

DO - 10.1006/jmbi.2001.5388

M3 - Article

C2 - 11884128

AN - SCOPUS:0036290278

SN - 0022-2836

VL - 316

SP - 875

EP - 885

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 4

ER -

Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli

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