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Information on EC 3.1.26.11 - tRNase Z and Organism(s) Arabidopsis thaliana and UniProt Accession Q8LGU7
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3.1.26.11 tRNase ZSpecify your search results
Word Map
- 3.1.26.11
- pre-trnas
- trailer
-
endonucleolytic
-
rnasel
- exoribonucleases
- metallo-beta-lactamase
-
pre-trna-like
-
two-line
-
3'-trailers
-
bisp-nitrophenylphosphate
-
trna-like
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule
Synonyms
elac2, trnase z, rnase z, rnase bn, trnase zl, 3' trnase, 3'-trnase, trnase zs, trna 3' processing endoribonuclease, rnase zs1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3 tRNase
-
-
-
-
3'-tRNA processing endoribonuclease
-
-
-
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nuclease, transfer ribonucleate maturation 3'-endoribo-(9CI)
-
-
-
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pre-tRNA processing endoribonuclease
-
-
-
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precursor tRNA 3'-end processing endoribonuclease
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-
-
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transfer RNA maturation endonuclease
-
-
-
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tRNA 3 endonuclease
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-
-
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tRNA 3' processing endoribonuclease
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-
-
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tRNA precursor-processing endoribonuclease
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-
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tRNase Z
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
98148-84-6
-
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
precursor tRNATyr + H2O
tRNA + 3' trailer
all four recombinant tRNase Z proteins have tRNA 3'-processing activity
-
-
?
IT1 + H2O
?
-
pre-tRNAIle with CCG and 50 nucleotide 3'-trailer sequence
-
-
?
IT2 + H2O
?
-
pre-tRNAIle with CUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT3 + H2O
?
-
pre-tRNAIle with UUG and 50 nucleotide 3'-trailer sequence
-
-
?
ITO + H2O
?
-
pre-tRNAIle with CCA and 50 nucleotide 3'-trailer sequence
-
-
?
S5L + H2O
?
-
pre-tRNATyr construct with 5 base pairs in the acceptor stem
-
-
?
S6L + H2O
?
-
pre-tRNATyr construct with 6 base pairs in the acceptor stem
-
-
?
S8L + H2O
?
-
pre-tRNATyr construct with 8 base pairs in the acceptor stem
-
-
?
S9L + H2O
?
-
pre-tRNATyr construct with 9 base pairs in the acceptor stem
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
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differentiation of tRNase Z variants by 3'-processing activity and their ability to hydrolyze the phosphodiester bond in the chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP), smallest known tRNase Z substrate, fourteen variants lost ability to hydrolyze bpNPP, seven variants reveal reduced activity
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
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differentiation of tRNase Z variants by the substrate bis(p-nitrophenyl)phosphate (bpNPP) described, smallest known tRNase Z substrate
-
-
?
precursor tRNATyr + H2O
tRNA + 3' trailer
all four recombinant tRNase Z proteins have tRNA 3'-processing activity
-
-
?
precursor tRNATyr + H2O
tRNA + 3' trailer
all four recombinant tRNase Z proteins have tRNA 3'-processing activity. TrZL2 processes the precursor less efficiently, which may be due to the fact that this enzyme is difficult to express and only low amounts of recombinant protein can be obtained
-
-
?
Rib3 + H2O
?
-
substrate with mature 5'tRNA and 3' unprocessed snoRNA
-
-
?
Rib3 + H2O
?
-
5' mature dicistronic tRNAGly-snoR43.1 precursor RNA
-
-
?
Rib4 + H2O
?
-
5' and 3' mature dicistronic tRNAGly-snoR43.1 precursor RNA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
0.2 mM, addition of Mn2+ ions triples activity, also required for in Vitro tRNA processing reactions
Zn2+
-
0.2 mM, addition of Zn2+ ions to the chelator-treated enzyme doubles activity, high affinity to Zn2+ even upon incubation with metal chelators, 0.76 Zn2+ ions retained per dimer
additional information
additional information
-
in contrast to bis(p-nitrophenyl)phosphate hydrolysis, pre-tRNA processing requires additional metal ions, Mn2+ or Mg2+, as Zn2+ ions alone are insufficient, metal dependence of the in vitro processing reaction analyzed, bis(p-nitrophenyl)phosphate activity of the chelator-treated AthTRZ1 without (TRZ-E) and with additional metal ions tested, chelator-treated AthTRZ1 without additional metal ions reveal same activity as the nonchelator-treated AthTRZ1
additional information
-
overview of the metal ion content in the active sites of tRNase Z and metallo-beta-lactamases, metal ion requirement by cleavage of bis(p-nitrophenyl)phosphate indicated, structure of metal binding site described, key residues of the zinc site identified by mutational studies summarized
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
reaction performed with 20 microM bis(p-nitrophenyl)phosphate and 20 microM tRNA, bis(p-nitrophenyl)phosphate does not inhibit tRNA binding
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
bis(p-nitrophenyl)phosphate
-
AthTRZ1-P178A, mutant, bis(p-nitrophenyl)phosphate catalysis
1.8
bis(p-nitrophenyl)phosphate
-
AthTRZ1-R252G, mutant, bis(p-nitrophenyl)phosphate catalysis
3.5
bis(p-nitrophenyl)phosphate
-
AthTRZ1-E208A, mutant, bis(p-nitrophenyl)phosphate catalysis
6
bis(p-nitrophenyl)phosphate
-
AthTRZ1-C40G, mutant, bis(p-nitrophenyl)phosphate catalysis
6.5
bis(p-nitrophenyl)phosphate
-
AthTRZ1-F51L, mutant, bis(p-nitrophenyl)phosphate catalysis
8
bis(p-nitrophenyl)phosphate
-
AthTRZ1-G62V, mutant, bis(p-nitrophenyl)phosphate catalysis
8.5
bis(p-nitrophenyl)phosphate
-
AthTRZ1 wild-type, hydrolysis of phosphodiester bonds of bpNPP, KM value for AthTRZ1 two-fold increased relative to that of the tRNase Z of Escherichia coli
13.2
bis(p-nitrophenyl)phosphate
-
AthTRZ1-C25G, mutant, bis(p-nitrophenyl)phosphate catalysis
22.2
bis(p-nitrophenyl)phosphate
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AthTRZ1-P64A, mutant, bis(p-nitrophenyl)phosphate catalysis
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover rate of AthTRZ1 eight-fold reduced if compared to tRNAse Z of Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
in vitro processing activities of different recombinant tRNase Z enzymes with respect to CCA-containing and CCA-less pre-tRNAs summarized
additional information
-
in vitro tRNA processing assays, bis(p-nitrophenyl)phosphate hydrolysis assay described, kinetic analysis shown, AthTRZ1 effective catalyst of bpNPP hydrolysis, AthTRZ1-R252G reveals ten times higher activity compared to the wild-type enzyme, in contrast to the short tRNase Z enzyme AthTRZ1, long tRNase Z enzymes do not have bis(p-nitrophenyl)phosphate hydrolysis activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
additional information
-
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1 and TrZL2
additional information
-
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
additional information
mRNAs corresponding to the tRNase Z proteins are found in all plant tissues. No significant variation between mRNA levels for TrZS1, TrZS2, TrZL1 and TrZL2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
The knockout TrZL1 mutant shows no visible phenotype
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2). TrZL1 is the only tRNase Z responsible for the maturation of nuclear tRNAs. The mitochondrial tRNase Z proteins TrZL1 cleave tRNA-like elements that serve as processing signals in mitochondrial mRNA maturation
malfunction
physiological function
malfunction
deletion of the chloroplastic TrZS2 gene results in an embryo-lethal phenotype
malfunction
The knockout TrZL2 and TrZS1 mutants show no visible phenotypes
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2)
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2). The mitochondrial tRNase Z protein TrZL2 cleaves tRNA-like elements that serve as processing signals in mitochondrial mRNA maturation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RNZ1_ARATH
280
0
31333
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C25G
dimerization, RNA binding, 33% activity compared to wild-type
C40G
dimerization, RNA binding, similar activity compared to wild-type
D185G
dimerization, RNA binding, 7% activity compared to wild-type
E208A
dimerization, RNA binding, 55% activity compared to wild-type
F51L
dimerization, RNA binding, similar activity compared to wild-type
G62V
dimerization, RNA binding, 26% activity compared to wild-type
L205I
weak dimerization, RNA binding, 56% activity compared to wild-type
P178A
dimerization, RNA binding, 74% activity compared to wild-type
P64A
dimerization, RNA binding, similar activity compared to wild-type
R252G
dimerization, RNA binding, 26% activity compared to wild-type
T210I
weak dimerization, RNA binding, 85% activity compared to wild-type
Y140L
weak dimerization, RNA binding, 30% activity compared to wild-type
Y253S
dimerization, RNA binding, 23% activity compared to wild-type
additional information
-
variants of tRNase Z enzymes generated by mutagenesis and properties of variants reviewed
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant TrZS1 purified. TrZL2 protein purified using the S tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
TrZL1 cloned into pBluescript KS II, subcloned into the NotI/XhoI sites of pET29 and expressed in Escherichia coli BL21-AI cells
expressed in Escherichia coli, prior to electrophoretic mobility shift assay (EMSA) and cross-linking experiments
-
TrZS1 expressed as described previously. TrZL2 cloned into pBluescript KS II, subcloned into the pET29 expression vector previously digested with BamHI/XhoI and expressed in Escherichia coli Rosetta cells
TrZS2 cloned into the pUC18 vector, subcloned into the NcoI/XhoI sites of pET32 expression vector and expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells as a fusion protein with both His and S tags
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
all tRNase Z genes are expressed during all growth stages of Arabidopsis, in particular during the first stage of development (seedling) and at the start of flowering
all tRNase Z genes are expressed during all growth stages of Arabidopsis, in particular during the first stage of development (seedling) and at the start of flowering
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
comparative studies both bis(p-nitrophenyl)phosphate hydrolysis and pre-tRNA processing of tRNase Z variants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kruszka, K.; Barneche, F.; Guyot, R.; Ailhas, J.; Meneau, I.; Schiffer, S.; Marchfelder, A.; Echeverria, M.
Plant dicistronic tRNA-snoRNA genes: a new mode of expression of the small nucleolar RNAs processed by RNase Z
EMBO J.
22
621-632
2003
Arabidopsis thaliana, Rattus norvegicus
Schiffer, S.; Rsch, S.; Marchfelder, A.
Assigning a function to a conserved group of proteins: the tRNA 3'-processing enzymes
EMBO J.
21
2769-2777
2002
Arabidopsis thaliana, Triticum aestivum (P60193), Triticum aestivum, Methanocaldococcus jannaschii (Q58897)
Schiffer, S.; Rosch, S.; Marchfelder, A.
Recombinant RNase Z does not recognize CCA as part of the tRNA and its cleavage efficiency is influenced by acceptor stem length
Biol. Chem.
384
333-342
2003
Arabidopsis thaliana, Methanocaldococcus jannaschii, Triticum aestivum
Vogel, A.; Schilling, O.; Spath, B.; Marchfelder, A.
The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
Biol. Chem.
386
1253-1264
2005
Arabidopsis thaliana, Arabidopsis thaliana (Q8L633), Arabidopsis thaliana (Q8LGU7), Arabidopsis thaliana (Q8VYS2), Bacillus subtilis (P54548), Caenorhabditis elegans (O44476), Drosophila melanogaster (Q8MKW7), Escherichia coli (P0A8V0), Haloferax volcanii, Homo sapiens (Q9BQ52), Homo sapiens (Q9H777), Methanocaldococcus jannaschii (Q58897), Pyrobaculum aerophilum (Q8ZTJ7), Pyrococcus furiosus (Q8U182), Saccharomyces cerevisiae (P36159), Thermoplasma acidophilum (Q9HJ19), Thermotoga maritima
Spath, B.; Kirchner, S.; Vogel, A.; Schubert, S.; Meinlschmidt, P.; Aymanns, S.; Nezzar, J.; Marchfelder, A.
Analysis of the functional modules of the tRNA 3' endonuclease (tRNase Z)
J. Biol. Chem.
280
35440-35447
2005
Arabidopsis thaliana (Q8LGU7)
Spaeth, B.; Settele, F.; Schilling, O.; DAngelo, I.; Vogel, A.; Feldmann, I.; Meyer-Klaucke, W.; Marchfelder, A.
Metal requirements and phosphodiesterase activity of tRNase Z enzymes
Biochemistry
46
14742-14750
2007
Arabidopsis thaliana, Drosophila melanogaster, Saccharomyces cerevisiae (P36159)
Spaeth, B.; Canino, G.; Marchfelder, A.
tRNase Z: the end is not in sight
Cell. Mol. Life Sci.
64
2404-2412
2007
Arabidopsis thaliana, Caenorhabditis elegans, Danio rerio, Drosophila melanogaster (Q8MKW7), Gallus gallus, Homo sapiens, Mus musculus, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Ceballos, M.; Vioque, A.
tRNase Z
Protein Pept. Lett.
14
137-145
2007
Synechocystis sp., Arabidopsis thaliana, Bacillus subtilis, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Thermotoga maritima
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