Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Mayer, M.; Schiffer, S.; Marchfelder, A.: tRNA 3′ processing in plants: nuclear and mitochondrial activities differ. Biochemistry, 39, 2096–2105 (2000)
Nashimoto, M.; Tamura, M.; Kaspar, R.L.: Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease. Biochemistry, 38, 12089–12096 (1999)
Nashimoto, M.: Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease. Nucleic Acids Res., 25, 1148–1154 (1997)
Nashimoto, M.; Geary, S.; Tamura, M.; Kaspar, R.: RNA heptamers that direct RNA cleavage by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 26, 2565–2571 (1998)
Nashimoto, M.; Wesemann, D.R.; Geary, S.; Tamura, M.; Kaspar, R.L.: Long 5′ leaders inhibit removal of a 3′ trailer from a precursor tRNA by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 27, 2770–2776 (1999)
Han, S.J.; Kang, H.S.: Purification and characterization of the precursor tRNA 3′-end processing nuclease from Aspergillus nidulans. Biochem. Biophys. Res. Commun., 233, 354–358 (1997)
Mörl, M.; Marchfelder, A.: The final cut. The importance of tRNA 3′-processing. EMBO Rep., 2, 17–20 (2001)
Mohan, A.; Whyte, S.; Wang, X.; Nashimoto, M.; Levinger, L.: The 3′ end CCA of mature tRNA is an antideterminant for eukaryotic 3′-tRNase. RNA, 5, 245–256 (1999)
Oommen, A.; Li, X.; Gegenheimer, P.: Cleavage specificity of chloroplast and nuclear tRNA 3′-processing nucleases. Mol. Cell. Biol., 12, 865–875 (1992)
Nashimoto, M.: Anomalous RNA substrates for mammalian tRNA 3′ processing endoribonuclease. FEBS Lett., 472, 179–186 (2000)
Nashimoto, M.; Tamura, M.; Kaspar, R.L.: Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease. J. Mol. Biol., 287, 727–740 (1999)
Schierling, K.; Roesch, S.; Rupprecht, R.; Schiffer, S.; Marchfelder, A.: tRNA 3′ end maturation in archaea has eukaryotic features: the RNase Z from Haloferax volcanii. J. Mol. Biol., 316, 895–902 (2002)
Kunzmann, A.; Brennicke, A.; Marchfelder, A.: 5′ End maturation and RNA editing have to precede tRNA 3′ processing in plant mitochondria. Proc. Natl. Acad. Sci. USA, 95, 108–113 (1998)
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)
Manam, S.; Van Tuyle, G.C.: Separation and characterization of 5′-and 3′-tRNA processing nucleases from rat liver mitochondria. J. Biol. Chem., 262, 10272–10279 (1987)
Schiffer, S.; Rösch, S.; Marchfelder, A.: Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes. EMBO J., 21, 2769–2777 (2002)
Schiffer, S.; Helm, M.; Theobald-Dietrich, A.; Giege, R.; Marchfelder, A.: The plant tRNA 3′ processing enzyme has a broad substrate spectrum. Biochemistry, 40, 8264–8272 (2001)
Minagawa, A.; Takaku, H.; Shibata, H.S.; Ishii, R.; Takagi, M.; Yokoyama, S.; Nashimoto, M.: Substrate recognition ability differs among various prokaryotic tRNase Zs. Biochem. Biophys. Res. Commun., 345, 385–393 (2006)
Shibata, H.S.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.: Unstructured RNA is a substrate for tRNase Z. Biochemistry, 45, 5486–5492 (2006)
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)
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)
Pellegrini, O.; Nezzar, J.; Marchfelder, A.; Putzer, H.; Condon, C.: Endonucleodytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis. EMBO J., 22, 4534–4543 (2003)
Kostelecky, B.; Pohl, E.; Vogel, A.; Schilling, O.; Meyer-Klaucke, W.: The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins. J. Bacteriol., 188, 1607–1614 (2006)
Ishii, R.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.; Yokoyama, S.: Crystal structure of the tRNA 3′ processing endoribonuclease tRNase Z from Thermotoga maritima. J. Biol. Chem., 280, 14138–14144 (2005)
Ceballos-Chavez, M.; Vioque, A.: Sequence-dependent cleavage site selection by RNase Z from the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem., 280, 33461–33469 (2005)
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)
Yan, H.; Zareen, N.; Levinger, L.: Naturally occurring mutations in human mitochondrial pre-tRNASer(UCN) can affect the transfer ribonuclease Z cleavage site, processing kinetics, and substrate secondary structure. J. Biol. Chem., 281, 3926–3935 (2006)
Zareen, N.; Yan, H.; Hopkinson, A.; Levinger, L.: Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding. J. Mol. Biol., 350, 189–199 (2005)
Li de la Sierra-Gallay, I.; Mathy, N.; Pellegrini, O.; Condon, C.: Structure of the ubiquitous 3′ processing enzyme RNase Z bound to transfer RNA. Nat. Struct. Mol. Biol., 13, 376–377 (2006)
de la Sierra-Gallay, I.L.; Pellegrini, O.; Condon, C.: Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z. Nature, 433, 657–661 (2005)
Dubrovsky, E.B.; Dubrovskaya, V.A.; Levinger, L.; Schiffer, S.; Marchfelder, A.: Drosophila RNase Z processes mitochondrial and nuclear pre-tRNA 3′ ends in vivo. Nucleic Acids Res., 32, 255–262 (2004)
Zareen, N.; Hopkinson, A.; Levinger, L.: Residues in two homology blocks on the amino side of the tRNase Z His domain contribute unexpectedly to pre-tRNA 3′ end processing. RNA, 12, 1104–1115 (2006)
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2009). tRNase Z. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85703-7_19
Download citation
DOI: https://doi.org/10.1007/978-3-540-85703-7_19
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-85702-0
Online ISBN: 978-3-540-85703-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)