Work

YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity

Year: 2007

Type: article

Abstract: Oligoribonuclease is the only RNase in Escherichia coli that is able to degrade RNA oligonucleotides five residues and shorter in length. Firmicutes including Bacillus subtilis do not have an Oligoribonuclease (Orn) homologous protein and it is not yet understood which proteins accomplish the equivalent function in these organisms. We had previously identified oligoribonucleases Orn from E. coli and its human homolog Sfn in a screen for proteins that are regulated by 3'-phosphoadenosine 5'-phosphate (pAp). Here, we identify YtqI as a potential functional analog of Orn through its interaction with pAp. YtqI degrades RNA oligonucleotides in vitro with preference for 3-mers. In addition, YtqI has pAp-phosphatase activity in vitro. In agreement with these data, YtqI is able to complement both orn and cysQ mutants in E. coli. An ytqI mutant in B. subtilis shows impairment of growth in the absence of cysteine, a phenotype resembling that of a cysQ mutant in E. coli. Phylogenetic distribution of YtqI, Orn and CysQ supports bifunctionality of YtqI.

Source: Nucleic Acids Research

DOI: 10.1093/nar/gkm462

Authors: Undine Mechold, Gang Fang, Saravuth Ngo, Vasily Ogryzko, Antoine Danchin

Institutions: Institut Pasteur, Institut Gustave Roussy, Department of Genomes & Genetics, Aspects métaboliques et systémiques de l'oncogénèse pour de nouvelles approches thérapeutiques

Language: English

Topic: Biochemical and Molecular Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,992

Funder: European Commission