Journal of Molecular Biology
Volume 255, Issue 3, 26 January 1996, Pages 349-355
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Communication
The N-terminal Domain of therneGene Product has RNase E Activity and is Non-overlapping with the Arginine-rich RNA-binding Site

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Abstract

Thernegene ofEscherichia coliencodes a 118 kDa protein that has ribonuclease E (RNase E) activity and binds RNA. A functionalrnegene product is essential for cell viability and for the processing and/or decay of a variety of RNA species, including 9 S RNA, mRNA and RNAI, the antisense RNA regulator of ColE1-type plasmid replication. By testing the ability of different segments of the Rne protein to catalyze RNA cleavage and to bind RNA, we found that the N-terminal half (residues 1 to 498) of Rne contains a catalytic function sufficient for site-specific cleavage of oligoribonucleotides and complex RNAs. The C-terminal half of the protein, which contains both an arginine-rich region (residues 597 to 684) that we show binds RNA and a segment that is essential for cell viability (residues 844 to 1061), had no detectable endoribonucleolytic activity. Our results, which map the catalytic domain of RNase E, indicate the existence of discrete functional domains within the multifaceted Rne protein.

Keywords

RNase E
rne(ams of hmp1) gene
endoribonucleolytic cleavage
RNA binding
RNA processing and decay

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