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

Identifieur interne : 000182 ( France/Analysis ); précédent : 000181; suivant : 000183

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

Auteurs : Undine Mechold ; Gang Fang ; Saravuth Ngo ; Vasily Ogryzko [France] ; Antoine Danchin

Source :

RBID : PMC:1935014

Descripteurs français

English descriptors

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.


Url:
DOI: 10.1093/nar/gkm462
PubMed: 17586819
PubMed Central: 1935014


Affiliations:


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Links to Exploration step

PMC:1935014

Le document en format XML

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<p>Oligoribonuclease is the only RNase in
<italic>Escherichia coli</italic>
that is able to degrade RNA oligonucleotides five residues and shorter in length. Firmicutes including
<italic>Bacillus subtilis</italic>
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
<italic>E. coli</italic>
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
<italic>in vitro</italic>
with preference for 3-mers. In addition, YtqI has pAp-phosphatase activity
<italic>in vitro</italic>
. In agreement with these data, YtqI is able to complement both
<italic>orn</italic>
and
<italic>cysQ</italic>
mutants in
<italic>E. coli</italic>
. An
<italic>ytqI</italic>
mutant in
<italic>B. subtilis</italic>
shows impairment of growth in the absence of cysteine, a phenotype resembling that of a
<italic>cysQ</italic>
mutant in
<italic>E. coli</italic>
. Phylogenetic distribution of YtqI, Orn and CysQ supports bifunctionality of YtqI.</p>
</div>
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</record>

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