Quaternary structure and biochemical properties of mycobacterial RNase E/G

Mirijam Elisabeth Zeller, Agnes Csanadi, A. Miczák, Thierry Rose, Thierry Bizebard, Vladimir R. Kaberdin

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

The RNase E/G family of endoribonucleases plays the central role in numerous post-transcriptional mechanisms in Escherichia coli and, presumably, in other bacteria, including human pathogens. To learn more about specific properties of RNase E/G homologues from pathogenic Gram-positive bacteria, a polypeptide comprising the catalytic domain of Mycobacterium tuberculosis RNase E/G (MycRne) was purified and characterized in vitro. In the present study, we show that affinity-purified MycRne has a propensity to form dimers and tetramere in solution and possesses an endoribonucleolytic activity, which is dependent on the 5′-phosphorylation status of RNA. Our data also indicate that the cleavage specificities of the M. tuberculosis RNase E/G homologue and its E. coli counterpart are only moderately overlapping, and reveal a number of sequence determinants within MycRne cleavage sites that differentially affect the efficiency of cleavage. Finally, we demonstrate that, similar to E. coli RNase E, MycRne is able to cleave in an intercistronic region of the putative 9S precursor of 5S rRNA, thus suggesting a common function for RNase E/G homologues in rRNA processing.

Original languageEnglish
Pages (from-to)207-215
Number of pages9
JournalBiochemical Journal
Volume403
Issue number1
DOIs
Publication statusPublished - Apr 1 2007

Fingerprint

Mycobacterium tuberculosis
Escherichia coli
Bacteria
Spiruroidea
Endoribonucleases
ribonuclease E
Phosphorylation
Intergenic DNA
RNA Precursors
Gram-Positive Bacteria
Pathogens
Dimers
Catalytic Domain
RNA
Peptides
Processing

Keywords

  • 5′-end-dependence
  • Escherichia coli
  • Mycobacterium tuberculosis
  • Ribonuclease
  • RNA processing
  • RNase E/G

ASJC Scopus subject areas

  • Biochemistry

Cite this

Zeller, M. E., Csanadi, A., Miczák, A., Rose, T., Bizebard, T., & Kaberdin, V. R. (2007). Quaternary structure and biochemical properties of mycobacterial RNase E/G. Biochemical Journal, 403(1), 207-215. https://doi.org/10.1042/BJ20061530

Quaternary structure and biochemical properties of mycobacterial RNase E/G. / Zeller, Mirijam Elisabeth; Csanadi, Agnes; Miczák, A.; Rose, Thierry; Bizebard, Thierry; Kaberdin, Vladimir R.

In: Biochemical Journal, Vol. 403, No. 1, 01.04.2007, p. 207-215.

Research output: Contribution to journalArticle

Zeller, ME, Csanadi, A, Miczák, A, Rose, T, Bizebard, T & Kaberdin, VR 2007, 'Quaternary structure and biochemical properties of mycobacterial RNase E/G', Biochemical Journal, vol. 403, no. 1, pp. 207-215. https://doi.org/10.1042/BJ20061530
Zeller, Mirijam Elisabeth ; Csanadi, Agnes ; Miczák, A. ; Rose, Thierry ; Bizebard, Thierry ; Kaberdin, Vladimir R. / Quaternary structure and biochemical properties of mycobacterial RNase E/G. In: Biochemical Journal. 2007 ; Vol. 403, No. 1. pp. 207-215.
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