YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity.
Identifieur interne : 002177 ( PubMed/Corpus ); précédent : 002176; suivant : 002178YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity.
Auteurs : Undine Mechold ; Gang Fang ; Saravuth Ngo ; Vasily Ogryzko ; Antoine DanchinSource :
- Nucleic acids research [ 1362-4962 ] ; 2007.
English descriptors
- KwdEn :
- Adenosine Diphosphate (metabolism), Bacillus subtilis (enzymology), Bacterial Proteins (classification), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Escherichia coli (genetics), Exoribonucleases (genetics), Exoribonucleases (metabolism), Genetic Complementation Test, Phosphoric Monoester Hydrolases (genetics), Phosphoric Monoester Hydrolases (metabolism), Phylogeny, RNA (metabolism), Substrate Specificity.
- MESH :
- chemical , classification : Bacterial Proteins.
- chemical , genetics : Bacterial Proteins, Exoribonucleases, Phosphoric Monoester Hydrolases.
- chemical , metabolism : Adenosine Diphosphate, Bacterial Proteins, Exoribonucleases, Phosphoric Monoester Hydrolases, RNA.
- enzymology : Bacillus subtilis.
- genetics : Escherichia coli.
- Genetic Complementation Test, Phylogeny, Substrate Specificity.
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.
DOI: 10.1093/nar/gkm462
PubMed: 17586819
Links to Exploration step
pubmed:17586819Le document en format XML
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17586819</PMID><DateCompleted><Year>2007</Year><Month>08</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>13</Issue><PubDate><Year>2007</Year></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity.</ArticleTitle><Pagination><MedlinePgn>4552-61</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mechold</LastName><ForeName>Undine</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15, France. umechold@pasteur.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Gang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Ngo</LastName><ForeName>Saravuth</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ogryzko</LastName><ForeName>Vasily</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Danchin</LastName><ForeName>Antoine</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research 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