Open AccessQuaternary structure and biochemical properties of mycobacterial RNase E/G
Author(s) -
Mirijam Elisabeth Zeller,
Ágnes Csanádi,
András Miczák,
Thierry Rose,
Thierry Bizebard,
Vladimir R. Kaberdin
Publication year - 2007
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bj20061530
Subject(s) - rnase p , rnase mrp , ribonuclease iii , escherichia coli , biology , cleavage (geology) , rnase h , rna , rnase ph , bacteria , biochemistry , ribonuclease , ribosomal rna , microbiology and biotechnology , genetics , gene , paleontology , rna interference , fracture (geology)
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 tetramers 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.