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J Biol Chem. 2014 Jan 24;289(4):2139-47. doi: 10.1074/jbc.M113.525683. Epub 2013 Dec 4.

Mycobacterium tuberculosis Rv2179c protein establishes a new exoribonuclease family with broad phylogenetic distribution.

Author information

1
From Emerald Bio, Bainbridge Island, Washington 98110.

Abstract

Ribonucleases (RNases) maintain the cellular RNA pool by RNA processing and degradation. In many bacteria, including the human pathogen Mycobacterium tuberculosis (Mtb), the enzymes mediating several central RNA processing functions are still unknown. Here, we identify the hypothetical Mtb protein Rv2179c as a highly divergent exoribonuclease. Although the primary sequence of Rv2179c has no detectable similarity to any known RNase, the Rv2179c crystal structure reveals an RNase fold. Active site residues are equivalent to those in the DEDD family of RNases, and Rv2179c has close structural homology to Escherichia coli RNase T. Consistent with the DEDD fold, Rv2179c has exoribonuclease activity, cleaving the 3' single-strand overhangs of duplex RNA. Functional orthologs of Rv2179c are prevalent in actinobacteria and found in bacteria as phylogenetically distant as proteobacteria. Thus, Rv2179c is the founding member of a new, large RNase family with hundreds of members across the bacterial kingdom.

KEYWORDS:

Annotation; Crystal Structure; Microbiology; Mycobacterium tuberculosis; Pseudomonas; Ribonuclease

PMID:
24311791
PMCID:
PMC3900960
DOI:
10.1074/jbc.M113.525683
[Indexed for MEDLINE]
Free PMC Article

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