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1,N6-etheno-2'-dApG + H2O
1,N6-etheno-2'-deoxyadenosine + GMP
24mer RNA + H2O
nucleoside 5'-phosphates
3'-phosphoadenosine 5'-phosphate + H2O
AMP + phosphate
-
-
-
-
?
4-nitrophenyl-TMP + H2O
4-nitrophenol + TMP
5'-CACACACACACACACACACACACA-3' + H2O
?
5'-p-nitrophenyl-TMP + H2O
p-nitrophenol + TMP
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
5'Cy5-CCCCC3' + H2O
?
5'Cy5-AAAAA3' is a better substrate than 5'Cy5-CCCCC3'
-
-
?
CpC + H2O
5'-CMP + cytidine
-
-
-
-
?
CpU + H2O
3'-CMP + uridine
-
-
-
-
?
dApG + H2O
2'-deoxyadenosine + GMP
DNA + H2O
nucleoside 5'-phosphates
mRNA + H2O
nucleoside 5'-phosphates
-
required for for degradation of mRNA to mononucleotides
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
p-nitrophenyl deoxythymidine 5'-phosphate + H2O
p-nitrophenol + 5'-TMP
-
no activity on nitrophenyl deoxythymidine 3'-phosphate
-
-
?
p-nitrophenyl uridine 5'-monophosphate + H2O
p-nitrophenol + 5'-UMP
-
-
-
-
?
p-nitrophenyl-2',3'-isopropyl-5'-UMP + H2O
p-nitrophenol + isopropyl-5'-UMP
-
-
-
-
?
polymer synthesized from NAD+ + H2O
?
-
chain length 27-30
-
-
?
RNA + H2O
nucleoside 5'-phosphate + ?
-
degrades RNA oligonucleotides with preference for 3-mers
-
-
?
RNA + H2O
nucleoside 5'-phosphates
UpC + H2O
5'-CMP + 5'-UMP
-
-
-
-
?
UpU + H2O
5'-UMP
-
-
-
-
?
additional information
?
-
(Ap)2 + H2O
?
-
-
-
-
?
1,N6-etheno-2'-dApG + H2O
1,N6-etheno-2'-deoxyadenosine + GMP
-
-
-
?
1,N6-etheno-2'-dApG + H2O
1,N6-etheno-2'-deoxyadenosine + GMP
-
-
-
?
1,N6-etheno-2'-dApG + H2O
1,N6-etheno-2'-deoxyadenosine + GMP
-
-
-
?
24mer RNA + H2O
nucleoside 5'-phosphates
-
-
-
?
24mer RNA + H2O
nucleoside 5'-phosphates
-
-
-
?
4-nitrophenyl-TMP + H2O
4-nitrophenol + TMP
artificial assay substrate
-
-
?
4-nitrophenyl-TMP + H2O
4-nitrophenol + TMP
artificial assay substrate
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-CACACACACACACACACACACACA-3' + H2O
?
-
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-Cy5-CCCCC-3' + H2O
?
low activity
-
-
?
5'-p-nitrophenyl-TMP + H2O
p-nitrophenol + TMP
-
-
-
-
?
5'-p-nitrophenyl-TMP + H2O
p-nitrophenol + TMP
-
-
-
-
?
5'-p-nitrophenyl-TMP + H2O
p-nitrophenol + TMP
-
-
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
-
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'-phosphoguanylyl-(3',5')-guanosine + H2O
GMP + guanosine
i.e. pGpG
-
-
?
5'Cy5-AAA3' + H2O
?
better substrate than 5'Cy5-CCCCC3'
-
-
?
5'Cy5-AAA3' + H2O
?
better substrate than 5'Cy5-CCCCC3'
-
-
?
5'Cy5-AAAAA3' + H2O
?
better substrate than 5'Cy5-CCCCC3'
-
-
?
5'Cy5-AAAAA3' + H2O
?
better substrate than 5'Cy5-CCCCC3'
-
-
?
5'Cy5-CCC3' + H2O
?
5'Cy5-AAA3' is a better substrate than 5'Cy5-CCC3'
-
-
?
5'Cy5-CCC3' + H2O
?
5'Cy5-AAA3' is a better substrate than 5'Cy5-CCC3'
-
-
?
dApG + H2O
2'-deoxyadenosine + GMP
-
-
-
?
dApG + H2O
2'-deoxyadenosine + GMP
-
-
-
?
dApG + H2O
2'-deoxyadenosine + GMP
-
-
-
?
DNA + H2O
nucleoside 5'-phosphates
-
no activity
-
-
?
DNA + H2O
nucleoside 5'-phosphates
-
active after dissociation from a ribonucleoprotein
-
-
?
DNA + H2O
nucleoside 5'-phosphates
-
hydrolyzed very slowly, not: ADP, UDP, ATP, UTP
-
-
?
NAD+ + H2O
NMN + AMP
-
-
-
-
?
NAD+ + H2O
NMN + AMP
-
-
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
-
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
processive degradation
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
however higher affinity to longer chains
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
exonuclease: 3`to 5'-direction
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
reaction rate inversely proportional to chain length of substrate
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
hydrolyzes oligodeoxyribonucleotides and oligoribonucleotides
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
specific for short ribooligonucleotides
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
initial site of attack: 3'-hydroxyl end
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
also hydrolyses NAD+ to NMN and AMP, mechanism
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
essential for complete degradation of mRNA
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
-
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
exonuclease: 3`to 5'-direction
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
hydrolyzes oligodeoxyribonucleotides and oligoribonucleotides
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
has higher affinity to shorter chains
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
no activity at 3'-phosphate end
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
hydrolyzes oligodeoxyribonucleotides and oligoribonucleotides
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
-
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
no base specificity
-
-
?
oligonucleotides + H2O
nucleoside 5'-phosphates
-
initial site of attack: 3'-hydroxyl end
-
-
?
RNA + H2O
nucleoside 5'-phosphates
-
active after dissociation from a ribonucleoprotein
-
-
?
RNA + H2O
nucleoside 5'-phosphates
-
hydrolyzed very slowly
-
-
?
additional information
?
-
oligo(A) RNA substrates are preferred over oligo(C) substrates, and RA 5mers are preferred over RNA 3mers
-
-
?
additional information
?
-
-
oligo(A) RNA substrates are preferred over oligo(C) substrates, and RA 5mers are preferred over RNA 3mers
-
-
?
additional information
?
-
oligo(A) RNA substrates are preferred over oligo(C) substrates, and RA 5mers are preferred over RNA 3mers
-
-
?
additional information
?
-
CpsORN activities on 5-mer RNA or DNA are determined using custom-made 5'-fluorescein-labelled oligonucleotides, and assay on 24-mer RNA oligonucleotide. Small RNA hydrolysis mechanism of CpsORN, mechanism, overview
-
-
?
additional information
?
-
CpsORN activities on 5-mer RNA or DNA are determined using custom-made 5'-fluorescein-labelled oligonucleotides, and assay on 24-mer RNA oligonucleotide. Small RNA hydrolysis mechanism of CpsORN, mechanism, overview
-
-
?
additional information
?
-
oligoribonuclease is a common downstream target of lithium-induced pAp accumulation (inhibition of the pAp-degrading enzyme by lithium is widely used to treat bipolar disorders)
-
-
?
additional information
?
-
-
oligoribonuclease is a common downstream target of lithium-induced pAp accumulation (inhibition of the pAp-degrading enzyme by lithium is widely used to treat bipolar disorders)
-
-
?
additional information
?
-
poor activity with 4-nitrophenyl phosphate
-
-
?
additional information
?
-
-
oligoribonuclease is a common downstream target of lithium-induced pAp accumulation (inhibition of the pAp-degrading enzyme by lithium is widely used to treat bipolar disorders)
-
-
?
additional information
?
-
poor activity with 4-nitrophenyl phosphate
-
-
?
additional information
?
-
oligoribonuclease (Orn) is an exoribonuclease that hydrolyzes two- to five-nucleotide-long RNAs. Orn degrades short oligoRNAs regardless of sequence
-
-
?
additional information
?
-
-
oligoribonuclease (Orn) is an exoribonuclease that hydrolyzes two- to five-nucleotide-long RNAs. Orn degrades short oligoRNAs regardless of sequence
-
-
?
additional information
?
-
poor activity with 4-nitrophenyl phosphate
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
recombinant Orn degrades small RNAs in vitro, the enzyme has a proclivity for degrading RNA oligomers comprised of two to five nucleotides (nanoRNAs), including 5'-phosphoguanylyl-(3',5')-guanosine. Orn preferentially degrades purine dinucleotides in vitro. Exonuclease assays are carried out using 33P- and Cy5-labled RNA oligomer substrates. Orn is a calcium-insensitive exoribonuclease that selectively degrades purine rich nanoRNAs. (A) Degradation of the 24-mer 5'-33P-CACACACACA-CACACACACACACA-3'. Orn is a poor degrader of cytosine-rich nanoRNA substrates
-
-
?
additional information
?
-
-
degradation of RNA oligomers by oligoribonuclease is critical for completion of the Streptomyces coelicolor life cycle, but expression of ornA is not likely to be contigent on bldA-dependent translation of adpA
-
-
?
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evolution
Orn is a highly conserved 3'-to-5' exonuclease
evolution
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
evolution
-
Orn is highly conserved among bacteria but is not likely the only nano-RNAse important for cyclic diguanylate signal transduction
-
malfunction
mutation of gene orn leads to the accumulation of pGpG, which inhibits the function of glutamate-alanine-leucine (EAL) domain-containing enzymes, resulting in increased levels of cyclic-di-GMP and the consequent hyperbiofilm phenotype. EAL domain-containing enzymes hydrolyze cyclic-di-GMP to 5'-phosphoguanylyl-(3',5')-guanosine (pGpG). Mutation of orn drastically increases bacterial susceptibility to quinolones but not to tetracycline, aminoglycoside, or beta-lactam antibiotics. Upregulation of pyocin genes contributes to increased susceptibility to ciprofloxacin in the orn mutant. PrtR stability is reduced by the mutation of orn. Expression levels of prtN and PA0613 in wild-type and DELTAorn mutant strains PA14, phenotypes, overview
malfunction
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
malfunction
the lysates from DELTAorn show 25fold decrease in 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) hydrolysis. Complementation with wild-type, but not active site mutants, restores hydrolysis. Accumulation of pGpG in the DELTAorn strain inhibits PDE-As, increasing cyclic-diguanylate (c-di-GMP) concentration. Increased transcription from the cyclic-diguanylate-regulated pel promoter is observed. Additionally, the cyclic-diguanylate-governed auto-aggregation and biofilm phenotypes are elevated in the DELTAorn strain in a pel-dependent manner. Detection of elevated levels of pGpG and cyclic-diguanylate in the DELTAorn strain. Phenotype, overview
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
malfunction
-
Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
physiological function
depletion of isoform REXO2 by RNA interference causes a strong morphological phenotype in human cells, which show a disorganized network of punctate and granular mitochondria. Lack of REXO2 protein also causes a substantial decrease of mitochondrial nucleic acid content and impaires de novo mitochondrial protein synthesis
physiological function
-
expression of isoform NrnC in Escherichia coli can complement lack of oligoribonuclease Orn. Knock down of NrnC decreases the growth ability of Bartonella henselae
physiological function
bacterial oligoribonuclease (Orn) is a conserved 3'-to-5' exonuclease. In Pseudomonas aeruginosa, Orn plays a major role in the hydrolysis of pGpG, which is required for cyclic-di-GMP homeostasis. Orn is involved in the degradation of nanoRNAs, which can alter global gene expression by serving as transcription initiation primers. And Orn is required for the type III secretion system and pathogenesis of Pseudomonas aeruginosa, indicating a role of Orn in the bacterial response to environmental stimuli. Orn is required for the tolerance of Pseudomonas aeruginosa to ciprofloxacin, role of Orn in bacterial resistance to antibiotics. And role of Orn in genome integrity and bacterial resistance to quinolones. Oligoribonuclease is required for bacterial resistance to fluoroquinolones
physiological function
cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation
physiological function
oligoribonuclease (Orn), an exoribonuclease that hydrolyzes two- to five-nucleotide-long RNAs, is the primary enzyme responsible for degrading 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) in cells. Orn binds to pGpG specifically and can cleave it into GMP. pGpG inhibits RocR phosphodiesterase activity by binding to the active site and competing for cyclic diguanylate binding in the active site, and excess pGpG extends cyclic diguanylate half-life in vitro
physiological function
oligoribonuclease (Orn), which had earlier been established as an essential enzyme in most bacteria involved in the recycling of RNA into ribonucleotides, acts as c-di-GMP PDB-B in Pseudomonas aeruginosa cleaving diguanylate into (pGpG), and pGpG then into GMP
physiological function
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
-
the oligoribonuclease (Orn) is a manganese-dependent 3'->5' exonuclease that produces 5'-phosphorylated ribonucleotide monomers from polyribonucleotides, and it is important in providing homeostatic control of intracellular pGpG under native physiological conditions as well as in cyclic diguanylate (c-di-GMP) signaling in Pseudomonas aeruginosa. It is the primary enzyme responsible for 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) degradation in Pseudomonas aeruginosa cells, it degrades pGpG and prevents its accumulation in the bacterial cells. pGpG reduces the rate of c-di-GMP degradation in cell lysates and inhibits the activity of EAL-dependent phosphodiesterases (PA2133, PvrR, and purified recombinant RocR) from Pseudomonas aeruginosa. pGpG-dependent inhibition is alleviated by the addition of Orn. Orn is essential for the viability of Escherichia coli
-
physiological function
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cells regulate their intracellular mRNA levels by using specific ribonucleases. Oligoribonuclease (ORN) is a 3'-5' exoribonuclease for small RNA molecules, important in RNA degradation and re-utilisation
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additional information
structure analysis, identification of active site structure and key residues responsible for enzymatic catalysis of CpsORN, the active site of CpsORN has a negatively charged surface, created by Asp12, Glu14, Asp112, and Asp163, overview. His66 is located near the active site and potentially stabilises the negative charge of the nucleotide. His66 residue also plays a significant role in the cleavage mechanism. His66 and His158 are completely conserved among other ORNs. Residues Ser108 and Tyr129 are not essential for the RNase activity of CpsORN
additional information
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structure analysis, identification of active site structure and key residues responsible for enzymatic catalysis of CpsORN, the active site of CpsORN has a negatively charged surface, created by Asp12, Glu14, Asp112, and Asp163, overview. His66 is located near the active site and potentially stabilises the negative charge of the nucleotide. His66 residue also plays a significant role in the cleavage mechanism. His66 and His158 are completely conserved among other ORNs. Residues Ser108 and Tyr129 are not essential for the RNase activity of CpsORN
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purified recombinant unliganded wild-type enzyme and pNP-TMP-bound D163A mutant, and uridine-bound wild-type and mutant enzymes, sitting drop vapour diffusion method, crystals of unliganded CpsORN are obtained from 15% w/v PEG 3350 and 0.1 M magnesium formate, 20°C, for larger single crystals, by hanging-drop vapour-diffusion method, the drop volume is increased from 200 nl to 0.001 ml against 0.5 ml reservoir solution, optimised single crystals are obtained in the same condition as that of initial screening. The crystals of pNP-TMP-bound CpsORN are observed under several conditions. Among them, the most suitable crystals are obtained from the 1.4 M ammonium tartrate dibasic and 0.1 M Tris, pH 8.5, condition. The crystals of linked RNA-bound form are obtained with 0.04 M citric acid, 0.06 M Bis-Tris propane pH 6.4, and 20% w/v PEG 3350. Crystals of uridine-bound form are obtained with 0.2 M potassium thiocyanate and 20% w/v PEG 3350. X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution, molecular replacement and modelling
belongs to space group I422, with unit cell parameters a = 213.1, b = 213.1, c = 149.2, 90.0, 90.0, 90.0, to 30.0-3.1 A resolution, opposing dimeric arrangement, with the catalytic DEDD residues from one monomer closely juxtaposed with a large basic patch on the other monomer
both native and selenomethionine-labeled enzyme
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belongs to space group P21, with unit cell parameters a = 49.9, b = 76.6, c = 61.7, 90.0, 93.55, 90.0, to 19.97-2.09 A resolution, opposing dimeric arrangement, with the catalytic DEDD residues from one monomer closely juxtaposed with a large basic patch on the other monomer
by sitting-drop vapor diffusion method, to a resolution of 2.1 A, orn monomer comprises 9 alpha-helices and 5 beta-strands, helix H is oriented opposingly from similar helices in all reported 3'-5' DNases discovered so far, possibly to prevent steric hindrance of accommodating oligoribonucleotide substrates. Amino acids Leu135, Leu143, Ile140, and Leu174 form a hydrophobic cluster, side chains of Glu142/Arg133 and Thr139/Asp136 form salt bridges and H-bonds in the dimer interface, while side chains of Arg145, and Lys157 interact with the ribose 2'-OH or phosphate oxygen atoms of U5 substrates
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sitting-drop vapour-diffusion method, 2.1 A resolution, crystals are tetragonal and belong to space group P4(3)2(1)2 with unit cell parameters a = b = 67.5 A, c = 89.8 A. One molecule is present per asymmetric unit
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D163A
site-directed mutagenesis, mutation of the catalytic residue, inactive mutant
H158A
site-directed mutagenesis, the mutant completely loses its hydrolytic cleavage ability
H66A
site-directed mutagenesis, mutation is located on the alpha2 helix, inactive mutant
S108A
site-directed mutagenesis, the mutant exhibits similar activity as the wild-type
S167A
site-directed mutagenesis, mutant exhibits similar activity as the wild-type
Y129A
site-directed mutagenesis, mutant exhibits similar activity as the wild-type
Y129F
site-directed mutagenesis, mutant exhibits similar activity as the wild-type
H158A
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site-directed mutagenesis, the mutant completely loses its hydrolytic cleavage ability
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S108A
-
site-directed mutagenesis, the mutant exhibits similar activity as the wild-type
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S167A
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site-directed mutagenesis, mutant exhibits similar activity as the wild-type
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Y129A
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site-directed mutagenesis, mutant exhibits similar activity as the wild-type
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Y129F
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site-directed mutagenesis, mutant exhibits similar activity as the wild-type
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D130A
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pJS94, encoding the catalytically inactive point mutant OrnA D130A does not suppress the phenotype of the Streptomyces coelicolor J3411 (DELTAornA::apr) null mutant
additional information
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ytqI mutant, shows impairment of growth in the absence of cysteine
additional information
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ORN mutant, shows growth defect, YtqI from Bacillus subtilis is able to complement the mutant
additional information
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
additional information
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construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
additional information
generation of enzyme mutant DELTAorn, mRNA levels of pyocin biosynthesis genes in the DELTAorn mutant compared to those in wild-type strain PA14. Mutation of orn drastically increases bacterial susceptibility to quinolones but not to tetracycline, aminoglycoside, or beta-lactam antibiotics. Upregulation of pyocin genes contributes to increased susceptibility to ciprofloxacin in the orn mutant. PrtR stability is reduced by the mutation of orn
additional information
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generation of enzyme mutant DELTAorn, mRNA levels of pyocin biosynthesis genes in the DELTAorn mutant compared to those in wild-type strain PA14. Mutation of orn drastically increases bacterial susceptibility to quinolones but not to tetracycline, aminoglycoside, or beta-lactam antibiotics. Upregulation of pyocin genes contributes to increased susceptibility to ciprofloxacin in the orn mutant. PrtR stability is reduced by the mutation of orn
additional information
generation of enzyme mutant DELTAorn. The lysates from DELTAorn show 25fold decrease in 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) hydrolysis. Complementation with wild-type, but not active site mutants, restores hydrolysis. Accumulation of pGpG in the DELTAorn strain inhibits PDE-As, increasing cyclic-diguanylate (c-di-GMP) concentration. Increased transcription from the cyclic-diguanylate-regulated pel promoter is observed. Additionally, the cyclic-diguanylate-governed auto-aggregation and biofilm phenotypes are elevated in the DELTAorn strain in a pel-dependent manner. Detection of elevated levels of pGpG and cyclic-diguanylate in the DELTAorn strain
additional information
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generation of enzyme mutant DELTAorn. The lysates from DELTAorn show 25fold decrease in 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) hydrolysis. Complementation with wild-type, but not active site mutants, restores hydrolysis. Accumulation of pGpG in the DELTAorn strain inhibits PDE-As, increasing cyclic-diguanylate (c-di-GMP) concentration. Increased transcription from the cyclic-diguanylate-regulated pel promoter is observed. Additionally, the cyclic-diguanylate-governed auto-aggregation and biofilm phenotypes are elevated in the DELTAorn strain in a pel-dependent manner. Detection of elevated levels of pGpG and cyclic-diguanylate in the DELTAorn strain
additional information
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construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
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additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
-
construction of an enzyme knockout mutant by gene replacement, Pseudomonas aeruginosa DELTAorn mutant has high intracellular cyclic diguanylate (c-di-GMP) levels, causing this strain to overexpress extracellular polymers and overproduce biofilm. Mutant DELTAorn cells possess highly elevated 5'-phosphoguanylyl-(3',5')-guanosine (pGpG) levels
-
additional information
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oligoribonuclease null mutant J3411 (DELTAornA::apr), reveals a conditional defect in morphological differentiation that is reminiscent of bldA. PpJS93, containing ornA under the control of a constitutive promoter, completely suppresses the phenotype of Streptomyces coelicolor J3411 (DELTAornA::apr), but pJS94 (encoding catalytically inactive OrnA D130A) does not
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