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Information on EC 6.5.1.8 - 3'-phosphate/5'-hydroxy nucleic acid ligase
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6.5.1.8 3'-phosphate/5'-hydroxy nucleic acid ligaseIUBMB Comments
The enzyme is a GTP- and Mn2+-dependent 3'-5' nucleic acid ligase with the ability to join RNA with 3'-phosphate or 2',3'-cyclic-phosphate ends to RNA with 5'-hydroxy ends. It can also join DNA with 3'-phosphate ends to DNA with 5'-hydroxy ends, provided the DNA termini are unpaired . The enzyme is found in members of all three kingdoms of life, and is essential in metazoa for the splicing of intron-containing tRNAs. The reaction follows a three-step mechanism with initial activation of the enzyme by GTP hydrolysis, forming a phosphoramide bond between the guanylate and a histidine residue. The guanylate group is transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [DNA/RNA]-3'-(5'-diphosphoguanosine). When a suitable 5'-OH end is available, the enzyme catalyses an attack of the 5'-OH on the capped end to form a 3'-5' phosphodiester splice junction, releasing the guanylate. When acting on an RNA 2',3'-cyclic-phosphate, the enzyme catalyses an additional reaction, hydrolysing the cyclic phosphate to a 3'-phosphate . The metazoan enzyme requires activating cofactors in order to achieve multiple turnover catalysis .
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
5'-hydroxy-(ribonucleotide)m
+
=
+
+
+
+
+
=
+
+
(ribonucleotide)n-2',3'-cyclophosphate
+
5'-hydroxy-(ribonucleotide)m
+
+
=
+
+
Synonyms
rtcb-1, rtcb1, rtcb rna ligase, trna-splicing ligase, rna-splicing ligase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-P RNL
MXAN_0280
MXAN_4982
RNA-splicing ligase
rtcB
Rtcb-1
RtcB1
Trl1
tRNA splicing ligase
rtcB
-
-
-
-
rtcB
-
subunit of tRNA splicing ligase, also known as HSPC117, C22orf28, FAAP, or D10Wsu52e
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O = (ribonucleotide)n+m + GMP + diphosphate
(2) overall reaction
-
-
-
(ribonucleotide)n-2',3'-cyclophosphate + H2O = (ribonucleotide)n-3'-phosphate
(2a)
-
-
-
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m = (ribonucleotide)n+m + GMP
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP = (ribonucleotide)n+m + GMP + diphosphate
(1) overall reaction
-
-
-
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate = (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
GTP + [RNA ligase]-L-histidine = 5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
[RNA ligase]-Ntau-(5'-guanosyl-phosphono)-L-histidine + (ribonucleotide)n-3'-phosphate = (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
(2c)
-
-
-
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m = (ribonucleotide)n+m + GMP
(1c)
-
-
-
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m = (ribonucleotide)n+m + GMP
(2d)
-
-
-
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate = (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
(1b)
-
-
-
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate = (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
catalytic reaction mechanism, detailed overview
-
-
-
GTP + [RNA ligase]-L-histidine = 5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
(1a)
-
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-
GTP + [RNA ligase]-L-histidine = 5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
(2b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
poly(ribonucleotide)-3'-phosphate:5'-hydroxy-poly(ribonucleotide) ligase (GMP-forming)
The enzyme is a GTP- and Mn2+-dependent 3'-5' nucleic acid ligase with the ability to join RNA with 3'-phosphate or 2',3'-cyclic-phosphate ends to RNA with 5'-hydroxy ends. It can also join DNA with 3'-phosphate ends to DNA with 5'-hydroxy ends, provided the DNA termini are unpaired [6]. The enzyme is found in members of all three kingdoms of life, and is essential in metazoa for the splicing of intron-containing tRNAs. The reaction follows a three-step mechanism with initial activation of the enzyme by GTP hydrolysis, forming a phosphoramide bond between the guanylate and a histidine residue. The guanylate group is transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [DNA/RNA]-3'-(5'-diphosphoguanosine). When a suitable 5'-OH end is available, the enzyme catalyses an attack of the 5'-OH on the capped end to form a 3'-5' phosphodiester splice junction, releasing the guanylate. When acting on an RNA 2',3'-cyclic-phosphate, the enzyme catalyses an additional reaction, hydrolysing the cyclic phosphate to a 3'-phosphate [9]. The metazoan enzyme requires activating cofactors in order to achieve multiple turnover catalysis [8].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + dGTP
(ribonucleotide)20 + dGMP + diphosphate
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + GTP
(ribonucleotide)20 + GMP + diphosphate
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + ITP
(ribonucleotide)20 + IMP + diphosphate
(ribonucleotide)20-3'-phosphate + 5'-hydroxy-(ribonucleotide)20 + GTP
(ribonucleotide)40 + GMP + diphosphate
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + ATP + H2O
(ribonucleotide)n+m + AMP + diphosphate
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + CTP + H2O
(ribonucleotide)n+m + CMP + diphosphate
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + UTP + H2O
(ribonucleotide)n+m + UMP + diphosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m + GMP
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + 2-aminopurine-riboside-5'-triphosphate
(ribonucleotide)n+m + 2-aminopurine-riboside-5'-monophosphate + diphosphate
-
about 20% activity with 0.1 mM 2-aminopurine triphosphate compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + 2-mercaptopurine-riboside-5'-triphosphate
(ribonucleotide)n+m + 2-mercaptopurine-riboside-5'-monophosphate + diphosphate
-
about 25% activity with 0.1 mM 2-mercaptopurine triphosphate compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + 6-chloropurine-riboside-5'-triphosphate
(ribonucleotide)n+m + 6-chloropurine-riboside-5'-monophosphate + diphosphate
-
about 1% activity with 0.1 mM 6-chloropurine triphosphate compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + 6-O-methylguanosine triphosphate
(ribonucleotide)n+m + 6-O-methylguanosine phosphate + diphosphate
-
about 45% activity with 0.1 mM 6-O-methyl triphosphate compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + ATP
(ribonucleotide)n+m + AMP + diphosphate
-
about 22% activity with 0.1 mM ATP compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + CTP
(ribonucleotide)n+m + CMP + diphosphate
-
about 18% activity with 0.1 mM CTP compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + ITP
(ribonucleotide)n+m + IMP + diphosphate
-
about 75% activity with 0.1 mM ITP compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + UTP
(ribonucleotide)n+m + UMP + diphosphate
-
about 85% activity with 0.1 mM UTP compared to GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-phospho-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
overall reaction
-
?
(truncated 16S rRNA)-3'-phosphate + 5'-hydroxy-RNA43 + GTP
16S rRNA + GMP + diphosphate
-
endoribonuclease MazF, the toxin component of the toxin-antitoxin module mazEF, specifically cleaves the 16S rRNA of 70S ribosomes at an ACA site located at positions 15001502. Thereby, the ribosome loses a 3'-terminal 16S rRNA fragment of 43 nucleotides. RNA ligase RtcB catalyzes the religation of the truncated 16S rRNA present in specialized ribosomes. Thereby their ability to translate canonical mRNAs is fully restored
-
-
?
5'-guanosyl [RNA ligase]-NT-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
-
RtcB transfers GMP to the RNA 3'-phosphate end
-
?
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
GTP + [RNA ligase]-L-histidine
5'-guanosyl [RNA ligase]-NT-phosphono-L-histidine + diphosphate
-
-
-
?
GTP + [RNA ligase]-L-histidine
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + dGTP
(ribonucleotide)20 + dGMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + dGTP
(ribonucleotide)20 + dGMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + GTP
(ribonucleotide)20 + GMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + GTP
(ribonucleotide)20 + GMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + ITP
(ribonucleotide)20 + IMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + ITP
(ribonucleotide)20 + IMP + diphosphate
in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP
-
-
?
(ribonucleotide)20-3'-phosphate + 5'-hydroxy-(ribonucleotide)20 + GTP
(ribonucleotide)40 + GMP + diphosphate
-
-
overall reaction, phosphodiester bond synthesis is rate limiting
-
?
(ribonucleotide)20-3'-phosphate + 5'-hydroxy-(ribonucleotide)20 + GTP
(ribonucleotide)40 + GMP + diphosphate
-
-
overall reaction
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m
generation of substrate by cleavage of the intron-containing pre-tRNA with the Methanocaldococcus jannaschii tRNA splicing endonuclease
RtcB-catalyzed ligation incorporates the phosphate of the cyclic phosphate into the phosphodiester bond. ATP or GTP is not required
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m
generation of substrate by cleavage of the intron-containing pre-tRNA with the Methanocaldococcus jannaschii tRNA splicing endonuclease
RtcB-catalyzed ligation incorporates the phosphate of the cyclic phosphate into the phosphodiester bond. ATP or GTP is not required
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m
generation of substrate by cleavage of the intron-containing pre-tRNA with the Methanocaldococcus jannaschii tRNA splicing endonuclease
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m
generation of substrate by cleavage of the intron-containing pre-tRNA with the Methanocaldococcus jannaschii tRNA splicing endonuclease
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + ATP + H2O
(ribonucleotide)n+m + AMP + diphosphate
about 78% activity with 0.1 mM ATP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + ATP + H2O
(ribonucleotide)n+m + AMP + diphosphate
about 60% activity with 0.1 mM ATP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + ATP + H2O
(ribonucleotide)n+m + AMP + diphosphate
about 60% activity with 0.1 mM ATP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + CTP + H2O
(ribonucleotide)n+m + CMP + diphosphate
about 70% activity with 0.1 mM CTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + CTP + H2O
(ribonucleotide)n+m + CMP + diphosphate
about 60% activity with 0.1 mM CTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + CTP + H2O
(ribonucleotide)n+m + CMP + diphosphate
about 60% activity with 0.1 mM CTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
about 80% activity with 0.01 mM GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
about 75% activity with 0.01 mM GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
about 75% activity with 0.01 mM GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
substrate for ligation is a 20mer RNA strand with 5'-OH and 2',3'-cyclic phosphate ends
overall reaction
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
substrate mimicks the broken tRNAGlu(UUC) anticodon stem-loop generated by Kluyveromyces lactis gamma-toxin, leaving 2',3'-cyclic phosphate and 5'-OH ends
overall reaction
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
overall reaction
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + UTP + H2O
(ribonucleotide)n+m + UMP + diphosphate
about 75% activity with 0.1 mM UTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + UTP + H2O
(ribonucleotide)n+m + UMP + diphosphate
about 60% activity with 0.1 mM UTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + UTP + H2O
(ribonucleotide)n+m + UMP + diphosphate
about 60% activity with 0.1 mM UTP compared to GTP
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + H2O
(ribonucleotide)n-3'-phosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + H2O
(ribonucleotide)n-3'-phosphate
-
-
-
?
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m + GMP
-
-
-
?
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + 5'-hydroxy-(ribonucleotide)m
(ribonucleotide)n+m + GMP
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
overall reaction, RtcB is required for ligation of endogenous intron-containing pre-tRNAs
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
100% activity with 0.01 mM GTP
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
overall reaction, substrate 5'-hydroxy-(ribonucleotide)m can be composed of all ribonucleotides or all deoxynucleotides
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + GTP
? + GMP
substrate is a 20-mer HORNAp
RtcB1 efficiently converts the linear substrate to a circular RNA species as a consequence of intramolecular ligation plus multimers
-
?
(ribonucleotide)n-3'-phosphate + GTP
? + GMP
substrate is a 20-mer HORNAp
RtcB2 efficiently converts the linear substrate to a circular RNA species as a consequence of intramolecular ligation plus multimers. Isoform Rtcb2 is 5fold less effectively than isoform RtcB1
-
?
(ribonucleotide)n-3'-phosphate + GTP
? + GMP
substrate is a 20-mer HORNAp
RtcB1 efficiently converts the linear substrate to a circular RNA species as a consequence of intramolecular ligation plus multimers
-
?
(ribonucleotide)n-3'-phosphate + GTP
? + GMP
substrate is a 20-mer HORNAp
RtcB2 efficiently converts the linear substrate to a circular RNA species as a consequence of intramolecular ligation plus multimers. Isoform Rtcb2 is 5fold less effectively than isoform RtcB1
-
?
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
-
-
-
?
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
substrate for ligation is a 20-mer RNA strand with 5'-OH and 3'-monophosphate ends
-
-
?
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate
(ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine
-
-
-
?
GTP + [RNA ligase]-L-histidine
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
-
-
-
?
GTP + [RNA ligase]-L-histidine
5'-guanosyl [RNA ligase]-Ntau-phosphono-L-histidine + diphosphate
-
-
-
?
additional information
?
-
-
ATP and CTP are at least 3 orders of magnitude less effective as phosphate donors compared to GTP
-
-
?
additional information
?
-
RtcB executes a three-step ligation pathway, consisting of reaction of His337 of the enzyme with GTP to form a covalent RtcB-(histidinyl-N)-GMP intermediate, transfer of guanylate to a polynucleotide 3'-phosphate to form a polynucleotide-(3')pp(5')G intermediate, and (iii) attack of a 5'-OH on the N(3')pp(5')G end to form the splice junction. Presence of GTP is required
-
-
?
additional information
?
-
RtcB seals broken tRNA-like stem-loop structures with 2',3'-cyclic phosphate and 5'-OH ends to form a splice junction with a 2'-OH, 3',5'-phosphodiester
-
-
?
additional information
?
-
sealing of a 2',3'-cyclic phosphate end by RtcB requires GTP, is contingent on formation of the RtcBGMP adduct, and involves a kinetically valid RNA(3')pp(5')G intermediate. RtcB catalyzes the hydrolysis of a 2',3'-cyclic phosphate to a 3'-phosphate at a rate that is at least as fast as the rate of ligation. NTP requirement for ligation is satisfied by GTP and 6-O-methyl guanosine triphosphate and inosine triphosphate. 6-chloropurine ribonucleoside triphosphate, 2-aminopurine ribonucleoside triphosphate and ATP are inactive
-
-
?
additional information
?
-
-
the enzyme joins RNA 2',3'-cyclic phosphate or RNA 3'-phosphate ends to 5'-OH RNA ends in a multistep pathway whereby the enzyme hydrolyzes RNA 2',3'-cyclic phosphate to RNA 3'-phosphate, transfers GMP from GTP to RNA 3'-phosphate to form to RNAppG, and directs the attack of 5'-OH on RNAppG to form a 3'-5' phosphodiester splice junction
-
-
?
additional information
?
-
isoform Rtcb1 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb1 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
-
isoform Rtcb1 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb2 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb2 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
-
isoform Rtcb2 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb1 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb1 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb2 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
isoform Rtcb2 displays DNA ligase and DNA 3'-capping activities on a 12-mer pDNAp strand
-
-
?
additional information
?
-
three-step mechanism for catalysis of the ligation of 3'-P and 5'-OH RNA termini by RtcB. In the activation step, cleavage of the phosphoanhydride bond between the alpha and beta phosphoryl groups of GTP occurs during transfer of GMP to the 3'-P terminus of an RNA strand to form a guanylylate-activated intermediate. In the cyclization step, the 2'-OH on the terminal ribose attacks the GMP-activated 3'-P to generate a 2',3'-cyclic phosphate and release GMP. In the ligation step, the 5'-OH terminus of a second RNA strand attacks the cyclic phosphate to form a 3',5'-phosphodiester bond
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
(ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
(ribonucleotide)n+m + GMP + diphosphate
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
additional information
Mn2+
prior to binding GTP, a single manganese ion is bound to RtcB
Mn2+
the RtcB/Mn2+ structure shows two Mn2+ ions at the active site. The enzyme's substrate-induced GTP binding site and the putative reactive RNA ends are in the vicinity of the binuclear Mn2+ active center
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
archease
-
archease stimulates the activity of the human tRNA ligase complex with high efficiency only in the presence of GTP
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Trauma, Nervous System
Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex.
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00018
(ribonucleotide)10-3'-phosphate
pH 7.0, 70°C, ligation reaction
-
0.00055
(ribonucleotide)10-3'-phosphate
pH 7.0, 70°C, presence of archease, ligation reaction
-
0.0122
(ribonucleotide)20-3'-phosphate
-
pH 7.4, 70°C, presence of archease
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
a subset of RtcB is associated with the endoplasmic reticulum
brenda
a subset of RtcB is associated with the nuclear envelope
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
RNAi knockdown of rtcb-1 lowers endoplasmic reticulum stress response in vivo
physiological function
physiological function
archease and RtcB from Pyrococcus horikoshii function in tandem, with Archease altering the catalytic properties of the RNA ligase. Catalytic concentrations of archease are sufficient to activate RtcB, and Archease accelerates both the RNA 3'-P guanylylation and ligation steps. Archease can alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently. RtcB variants that have inactivating substitutions in the guanine-binding pocket can be rescued by the addition of archease. Substitution of the archease metal-binding residues drastically reduces archease-dependent activation of RtcB
physiological function
enzyme catalyzes the GTP-dependent ligation of RNA with 3'-phosphate and 5'-hydroxyl termini. RtcB can ligate RNA cleaved by RNA endonucleases, which generate 2',3'-cyclic phosphate and then 3'-phosphate termini on one strand, and a 5'-hydroxyl terminus on another strand
physiological function
RtcB as the primary unfolded protein response RNA ligase. In RtcB knockout cells, unconventional XBP1 mRNA splicing is defective during ER stress. The RNA ligase activity of RtcB is directly required for the splicing of XBP1 mRNA
physiological function
-
RtcB from Thermobifida fusca is a single-turnover enzyme that is unable to be converted into a multiple-turnover ligase by archease from other organisms
physiological function
-
RtcB from Thermus thermophilus displays a strong dependency on Archease for maximal activity and can catalyze multiple turnovers only in the presence of archease. Archease from P. horikoshii can activate Thermus thermophilus RtcB
physiological function
RtcB guanylylation precedes the cyclic phosphodiesterase and 3'-phosphate ligase steps of the RNA splicing pathway
physiological function
RtcB is able in vivo to complement growth of yeast cells that lack the endogenous healing/sealing-type tRNA ligase Trl1. RtcB also protects yeast Trl1 mutant cells against a fungal ribotoxin that incises the anticodon loop of cellular tRNAs. RtcB can replace Trl1 as the catalyst of HAC1 mRNA splicing during the unfolded protein response
physiological function
RtcB ligates 3'-monophosphate and 5'-OH ends and has an intrinsic 2',3'-cyclic phosphodiesterase activity. The 2',3'-cyclic phosphodiesterase and ligase reactions both require manganese and are abolished by mutation of the RtcB active site. RtcB executes a unique two-step pathway of strand joining whereby the 2',3'-cyclic phosphodiester end is hydrolyzed to a 3'-monophosphate, which is then linked to the 5'-OH end to form the splice junction. The energy for the 3'-phosphate ligase activity is provided by GTP
physiological function
RtcB ligates the xbp-1 mRNA during the IRE-1 branch of the unfolded protein response. Without RtcB, protein stress results in the accumulation of unligated xbp-1 mRNA fragments, defects in the unfolded protein response, and decreased lifespan. RtcB also ligates endogenous pre-tRNA halves, and RtcB mutants have defects in growth and lifespan that can be bypassed by expression of pre-spliced tRNAs. Animals that lack RtcB have defects that are independent of tRNA maturation and the unfolded protein response
physiological function
upon ER stress, HAC1/XBP1 undergoes exon/intron-specific excision by inositol requiring enzyme 1 to remove an intron and liberate the 5' and 3' exons, which are ligated by tRNA ligase. Expression of RtcB alone in a Saccharomyces cerevisiae tRNA ligase mutant strain inefficiently complements HAC1/XBP1 splicing and the RtcB cofactor archease is required to promote enzymatic activity of RtcB to catalyse RNA ligation
physiological function
-
upon ER stress, HAC1/XBP1 undergoes exon/intron-specific excision by inositol requiring enzyme 1 to remove an intron and liberate the 5' and 3' exons, which are ligated by tRNA ligase. Expression of RtcB in a Saccharomyces cerevisiae tRNA ligase mutant strain is able to complement HAC1/XBP1 splicing
physiological function
-
fungal tRNA ligase Trl1 is an essential enzyme that repairs RNA breaks with 2',3'-cyclic-PO4 and 5'-OH ends inflicted during tRNA splicing and noncanonical mRNA splicing in the fungal unfolded protein response
physiological function
-
the enzyme is a critical regulator of neuronal growth potential and inhibits axon regeneration
physiological function
-
the enzyme operates during the unfolded protein response
physiological function
-
the enzyme operates during the unfolded protein response
physiological function
the enzyme operates during the unfolded protein response
physiological function
the enzyme operates during the unfolded protein response
physiological function
the enzyme operates during the unfolded protein response
physiological function
-
the enzyme protects Caenorhabditis elegans dopamine neurons from age-dependent degeneration induced by human alpha-synuclein or 6-hyroxydopamine
physiological function
-
the enzyme operates during the unfolded protein response
-
physiological function
-
archease and RtcB from Pyrococcus horikoshii function in tandem, with Archease altering the catalytic properties of the RNA ligase. Catalytic concentrations of archease are sufficient to activate RtcB, and Archease accelerates both the RNA 3'-P guanylylation and ligation steps. Archease can alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently. RtcB variants that have inactivating substitutions in the guanine-binding pocket can be rescued by the addition of archease. Substitution of the archease metal-binding residues drastically reduces archease-dependent activation of RtcB
-
Show AA Sequence and Transmembrane Helices (1709 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with GDP and Mg2+, sitting drop vapor diffusion method, using 0.2 M sodium dihydrogen phosphate, 20% (w/v) PEG3350
-
three structures of RtcB complexes that capture snapshots along the entire guanylylation pathway. RtcB in complex with Mn(II) and GTP analogue guanosine 5'-(alpha-thio)-triphosphate shows that Mn1 is poised to stabilize the pentavalent transition state of guanylylation while a second manganese ion (Mn2) is coordinated to a nonbridging oxygen of the gamma-phosphoryl group. The diphosphate leaving group of 5'-(alpha-thio)-triphosphate is oriented apically to His404 with the epsilon nitrogen poised for in-line attack on the alpha phosphorus atom. The structure of RtcB in complex with 5'-(alpha-thio)-triphosphate also reveals the network of hydrogen bonds that recognize GTP and shows significant conformational changes accompanying the binding of the cofactor. A structure of the enzymic histidine-GMP intermediate depicts the end of the guanylylation pathway
crystal structures of RtcB in complex with Mn2+ alone and together with a covalently bound GMP, to 1.6 A and 2.3 A resolution, respectively. The RtcB/Mn2+ structure shows two Mn2+ ions at the active site, and an array of sulfate ions nearby that indicate the binding sites of the RNA phosphate backbone. The structure of the RtcB-GMP/Mn2+ complex reveals the detailed geometry of guanylylation of histidine 404. The enzyme's substrate-induced GTP binding site and the putative reactive RNA ends are in the vicinity of the binuclear Mn2+ active center
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C78A
D75A
H168A
H185A
H280A
active, protein is able to complement a Saccharomyces cerevisiae Trl1 mutant
H281A
-
the mutant is impaired in overall 5'-OH-RNAp and 5'-OH-RNA-2',3'-cyclic phosphate ligation but is able to seal a preguanylylated substrate
H337A
H337N
H337Q
K299A
-
the mutant shows about 50% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
N167A
R189A
R341A
R345A
-
the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme
D75A
-
the mutation allows cyclic phosphodiester hydrolysis but cripples 3'-phosphate guanylylation
H168A
-
the mutant shows about 48% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
H185A
-
the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme
H337A
His337 is the site covalent guanylylation of RtcB, mutant is inactive
H337A
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
H337A
-
the mutant shows about 1% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
H337N
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
H337Q
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
N167A
-
the mutant shows about 65% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
R189A
-
the mutation slows the step of RNAppG/5'-OH RNA sealing by a factor of 200 compared to that with wild type enzyme while decreasing the rate of RNAppG formation by 3fold
R341A
-
the mutant shows about 10% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His60 Ni Superflow resin column chromatography and Superose-200 gel filtration
His60 Ni Superflow resin column chromatography and Superose-200 gel filtration
His60 Ni Superflow resin column chromatography and Superose-200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a Saccharomyces cerevisiae trl1DELTA mutant
expression in Escherichia coli
expression in Saccharomyces cerevisiae
exprression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RtcB mRNA is processed by endoribonuclease MazF and selectively translated during stress
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, N.; Shuman, S.
RtcB is the RNA ligase component of an Escherichia coli RNA repair operon
J. Biol. Chem.
286
7727-7731
2011
Escherichia coli (P46850)
brenda
Desai, K.K.; Raines, R.T.
tRNA ligase catalyzes the GTP-dependent ligation of RNA with 3-phosphate and 5-hydroxyl termini
Biochemistry
51
1333-1335
2012
Pyrococcus furiosus (Q8U0H4)
brenda
Desai, K.K.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
Structures of the noncanonical RNA ligase RtcB reveal the mechanism of histidine guanylylation
Biochemistry
52
2518-2525
2013
Pyrococcus furiosus (Q8U0H4)
brenda
Poothong, J.; Tirasophon, W.; Kaufman, R.
Functional analysis of the mammalian RNA ligase for IRE1 in the unfolded protein response
Biosci. Rep.
37
BSR20160574
2017
Escherichia coli, Homo sapiens (Q9Y3I0)
brenda
Kosmaczewski, S.G.; Edwards, T.J.; Han, S.M.; Eckwahl, M.J.; Meyer, B.I.; Peach, S.; Hesselberth, J.R.; Wolin, S.L.; Hammarlund, M.
The RtcB RNA ligase is an essential component of the metazoan unfolded protein response
EMBO Rep.
15
1278-1285
2014
Caenorhabditis elegans (P90838), Caenorhabditis elegans
brenda
Maughan, W.P.; Shuman, S.
Characterization of 3-phosphate RNA ligase paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus highlights DNA and RNA 5'-phosphate capping activity of RtcB3
J. Bacteriol.
197
3616-3624
2015
Myxococcus xanthus (Q1D2I5), Myxococcus xanthus (Q1DFL2), Myxococcus xanthus, Myxococcus xanthus DK 1622 (Q1D2I5), Myxococcus xanthus DK 1622 (Q1DFL2)
brenda
Tanaka, N.; Meineke, B.; Shuman, S.
RtcB, a novel RNA ligase, can catalyze tRNA splicing and HAC1 mRNA splicing in vivo
J. Biol. Chem.
286
30253-30257
2011
Escherichia coli (P46850)
brenda
Tanaka, N.; Chakravarty, A.K.; Maughan, B.; Shuman, S.
Novel mechanism of RNA repair by RtcB via sequential 2',3'-cyclic phosphodiesterase and 3'-phosphate/5'-hydroxyl ligation reactions
J. Biol. Chem.
286
43134-43143
2011
Escherichia coli (P46850)
brenda
Lu, Y.; Liang, F.X.; Wang, X.
A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB
Mol. Cell
55
758-770
2014
Mus musculus (Q99LF4)
brenda
Chakravarty, A.K.; Shuman, S.
The sequential 2',3'-cyclic phosphodiesterase and 3'-phosphate/5'-OH ligation steps of the RtcB RNA splicing pathway are GTP-dependent
Nucleic Acids Res.
40
8558-8567
2012
Escherichia coli (P46850)
brenda
Desai, K.K.; Cheng, C.L.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation
Nucleic Acids Res.
42
3931-3942
2014
Pyrococcus horikoshii (O59245), Pyrococcus horikoshii DSM 12428 (O59245)
brenda
Temmel, H.; Mueller, C.; Sauert, M.; Vesper, O.; Reiss, A.; Popow, J.; Martinez, J.; Moll, I.
The RNA ligase RtcB reverses MazF-induced ribosome heterogeneity in Escherichia coli
Nucleic Acids Res.
45
4708-4721
2017
Escherichia coli
brenda
Englert, M.; Sheppard, K.; Aslanian, A.; Yates, J.R.; Soell, D.
Archaeal 3-phosphate RNA splicing ligase characterization identifies the missing component in tRNA maturation
Proc. Natl. Acad. Sci. USA
108
1290-1295
2011
Pyrococcus horikoshii (O59245), Methanopyrus kandleri (Q8TUS2), Pyrobaculum aerophilum (Q8ZY09), Pyrobaculum aerophilum DSM 7523 (Q8ZY09), Pyrococcus horikoshii DSM 12428 (O59245), Methanopyrus kandleri DSM 6324 (Q8TUS2)
brenda
Englert, M.; Xia, S.; Okada, C.; Nakamura, A.; Tanavde, V.; Yao, M.; Eom, S.H.; Konigsberg, W.H.; Soell, D.; Wang, J.
Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3-terminal phosphate and 5-OH
Proc. Natl. Acad. Sci. USA
109
15235-15240
2012
Pyrococcus horikoshii (O59245), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O59245)
brenda
Chakravarty, A.K.; Subbotin, R.; Chait, B.T.; Shuman, S.
RNA ligase RtcB splices 3-phosphate and 5-OH ends via covalent RtcB-(histidinyl)-GMP and polynucleotide-(3)pp(5)G intermediates
Proc. Natl. Acad. Sci. USA
109
6072-6077
2012
Escherichia coli (P46850)
brenda
Desai, K.K.; Beltrame, A.L.; Raines, R.T.
Coevolution of RtcB and Archease created a multiple-turnover RNA ligase
RNA
21
1866-1872
2015
Thermus thermophilus, Thermobifida fusca
brenda
Maughan, W.; Shuman, S.
Distinct contributions of enzymic functional groups to the 2',3'-cyclic phosphodiesterase, 3'-phosphate guanylylation, and 3'-ppG/5'-OH ligation steps of the Escherichia coli RtcB nucleic acid splicing pathway
J. Bacteriol.
198
1294-1304
2016
Escherichia coli
brenda
Ray, A.; Zhang, S.; Rentas, C.; Caldwell, K.A.; Caldwell, G.A.
RTCB-1 mediates neuroprotection via XBP-1 mRNA splicing in the unfolded protein response pathway
J. Neurosci.
34
16076-16085
2014
Caenorhabditis elegans
brenda
Popow, J.; Jurkin, J.; Schleiffer, A.; Martinez, J.
Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors
Nature
511
104-107
2014
Homo sapiens
brenda
Peach, S.E.; York, K.; Hesselberth, J.R.
Global analysis of RNA cleavage by 5-hydroxyl RNA sequencing
Nucleic Acids Res.
43
e108
2015
Escherichia coli
brenda
Remus, B.S.; Goldgur, Y.; Shuman, S.
Structural basis for the GTP specificity of the RNA kinase domain of fungal tRNA ligase
Nucleic Acids Res.
45
12945-12953
2017
Candida albicans
brenda
Kosmaczewski, S.; Han, S.; Han, B.; Meyer, B.; Baig, H.; Athar, W.; Lin-Moore, A.; Koelle, M.; Hammarlund, M.
RNA ligation in neurons by RtcB inhibits axon regeneration
Proc. Natl. Acad. Sci. USA
112
8451-8456
2015
Caenorhabditis elegans
brenda
Nandy, A.; Saenz-Mendez, P.; Gorman, A.M.; Samali, A.; Eriksson, L.A.
Homology model of the human tRNA splicing ligase RtcB
Proteins
85
1983-1993
2017
Homo sapiens (Q9Y3I0)
brenda
Remus, B.S.; Schwer, B.; Shuman, S.
Characterization of the tRNA ligases of pathogenic fungi Aspergillus fumigatus and Coccidioides immitis
RNA
22
1500-1509
2016
Coccidioides immitis (J3K151), Aspergillus fumigatus (Q4WTD4), Coccidioides immitis RS (J3K151)
brenda
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