3.1.26.11: tRNase Z
This is an abbreviated version!
For detailed information about tRNase Z, go to the full flat file.
Reaction
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
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Synonyms
(tRNase) Z, 3 tRNase, 3' tRNase, 3'-tRNA processing endoribonuclease, 3'-tRNase, AthTrz1, AthTrz2, AthTrz3, AthTrz4, BsuTrz, CelTrz, DmeTrz, EcoTrz, EcoZ, Elac, Elac1, ELAC2, HsaTrz1, HsaTrz2, HvoTrz, long form of 3' tRNase, long form of tRNA 3' processing endoribonuclease, long form of tRNase Z, MjaTrz, nuclease, transfer ribonucleate maturation 3'-endoribo-(9CI), PaeTrz, pre-tRNA processing endoribonuclease, precursor tRNA 3'-end processing endoribonuclease, ribonuclease Z, RNase BN, RNase Z, RNase ZL, RNase ZS1, RNaseZ, RNZ, SceTrz, SpTrz1p, SpTrz2p, TM0207, TmaTrz, TMS5 protein, transfer RNA maturation endonuclease, tRNA 3 endonuclease, tRNA 3' processing endoribonuclease, tRNA 3'-processing enzyme tRNase Z, tRNA precursor-processing endoribonuclease, tRNase Z, tRNase Z2, tRNase ZL, tRNase ZS, tRNaseZ, tRnaseZL, tRnaseZS, Trz, TRZ1, Trz1p, TRZ2, TrZL1, TrZL2, TrZS1, TrZS2, YP_145327, YqiK, YqjK, zinc phosphodiesterase, zinc-dependent phosphodiesterase, ZiPD
ECTree
Subunits
Subunits on EC 3.1.26.11 - tRNase Z
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x * 45000, SDS-PAGE
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x * 43000, mitochondrial RNase Z, SDS-PAGE
dimer
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dimer
cross-linking, SDS-PAGE
dimer
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homodimer, crystal structure
dimer
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homodimer, crystal structure
dimer
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crystallization, active site located near the dimer interface, flexible arm clamping the tRNA protrudes from the core into solution
dimer
gel filtration analysis shows that, only 20% of tRNase Z2 molecules form dimers, while tRNase Z molecules exist as dimers. This inefficient tRNase Z2 dimer formation may be attributed to the lack of alpha1, alpha2, and alpha3 that are important for dimerization of tRNase Z
dimer
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gel filtration analysis shows that, only 20% of tRNase Z2 molecules form dimers, while tRNase Z molecules exist as dimers. This inefficient tRNase Z2 dimer formation may be attributed to the lack of alpha1, alpha2, and alpha3 that are important for dimerization of tRNase Z
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homodimer
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alpha2, 2 * 41000, SDS-PAGE
homodimer
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crystallography
homodimer
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crystallography
homodimer
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crystallography
homodimer
alpha2, 2 * 43000, SDS-PAGE
monomer
1 * 90000, SDS-PAGE
monomer
1 * 92000, SDS-PAGE
monomer
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1 * 81892-83708, long isoform, MALDI-TOF mass spectrometry
monomer
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1 * 81904-83671, long isoform, calculated from amino acid sequence
monomer
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1 * 84000, long isoform, SDS-PAGE
monomer
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1 * 86997, long isoform, calculated from amino acid sequence
monomer
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1 * 87004, long isoform, MALDI-TOF mass spectrometry
additional information
the short form of tRNase Z, tRNase ZS, functions as a homodimer and is found in all prokaryotes and some eukaryotes. The long form, tRNase ZL, related to tRNase ZS through tandem duplication and found only in eukaryotes, possesses about 2000fold greater catalytic efficiency than tRNase ZS. tRNase ZL consists of related but diverged amino and carboxy domains connected by a flexible linker (also referred to as a flexible tether) and functions as a monomer. Biochemical exploration regions of Drosophila melanogaster tRNase Z through Ala scanning mutagenesis followed by processing kinetics is aided by analysis of flexibility using limited proteolysis and two-dimensional protein electrophoresis. This approach, informed by interpretation of a recent crystal structure of the Saccharomaces cerevisiae homolog, uncovers a hydrophobic subdomain formed across the amino domain-linker boundary, leading to the suggestion that peripheral substitutions affect the skeleton of twisted beta sheets in the amino domain on both sides of the flexible arm
additional information
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the short form of tRNase Z, tRNase ZS, functions as a homodimer and is found in all prokaryotes and some eukaryotes. The long form, tRNase ZL, related to tRNase ZS through tandem duplication and found only in eukaryotes, possesses about 2000fold greater catalytic efficiency than tRNase ZS. tRNase ZL consists of related but diverged amino and carboxy domains connected by a flexible linker (also referred to as a flexible tether) and functions as a monomer. Biochemical exploration regions of Drosophila melanogaster tRNase Z through Ala scanning mutagenesis followed by processing kinetics is aided by analysis of flexibility using limited proteolysis and two-dimensional protein electrophoresis. This approach, informed by interpretation of a recent crystal structure of the Saccharomaces cerevisiae homolog, uncovers a hydrophobic subdomain formed across the amino domain-linker boundary, leading to the suggestion that peripheral substitutions affect the skeleton of twisted beta sheets in the amino domain on both sides of the flexible arm
additional information
Trz1, Nuc1 and mutarotase form a very stable heterohexamer, composed of two copies of each of the three subunits. A Nuc1 homodimer is at the center of the complex, creating a two-fold symmetry and interacting with both Trz1 and mutarotase. Enzymatic characterization of the ternary complex revealed that the activities of Trz1 and mutarotase are not affected by complex formation, but that the Nuc1 activity is completely inhibited by mutarotase and partially by Trz1. This suggests that mutarotase and Trz1 might be regulators of the Nuc1 apoptotic nuclease activity
additional information
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Trz1, Nuc1 and mutarotase form a very stable heterohexamer, composed of two copies of each of the three subunits. A Nuc1 homodimer is at the center of the complex, creating a two-fold symmetry and interacting with both Trz1 and mutarotase. Enzymatic characterization of the ternary complex revealed that the activities of Trz1 and mutarotase are not affected by complex formation, but that the Nuc1 activity is completely inhibited by mutarotase and partially by Trz1. This suggests that mutarotase and Trz1 might be regulators of the Nuc1 apoptotic nuclease activity