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

被引：26

作者：

Lüttgen, H

Robelek, R

Mühlberger, R

Diercks, T

Schuster, SC

Köhler, P

Kessler, H

Bacher, A

Richter, G

机构：

[1] Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany

[2] Tech Univ Munich, Lehrstuhl Organ Chem 2, D-85747 Garching, Germany

[3] Max Planck Inst Biochem, Abt Membranbiochem, D-82152 Marinsried, Germany

[4] Tech Univ Munich, Inst Lebensmittelchem, D-85747 Garching, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 316卷 / 04期

关键词：

antitermination; ribosomal RNA; NMR spectroscopy; surface plasmon spectroscopy; protein/RNA interaction;

D O I：

10.1006/jmbi.2001.5388

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 H-1,N-15 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. (C) 2002 Elsevier Science Ltd.

引用

页码：875 / 885

页数：11

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