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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

Online
ISSN
1437-4315
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Volume 386, Issue 12

Issues

The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties

Andreas Vogel / Oliver Schilling
  • Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver V6T 1Z3, Canada
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Bettina Späth / Anita Marchfelder
Published Online: 2005-12-09 | DOI: https://doi.org/10.1515/BC.2005.142

Abstract

tRNase Z is the endoribonuclease that generates the mature 3′-end of tRNA molecules by removal of the 3′-trailer elements of precursor tRNAs. This enzyme has been characterized from representatives of all three domains of life (Bacteria, Archaea and Eukarya), as well as from mitochondria and chloroplasts. tRNase Z enzymes come in two forms: short versions (280–360 amino acids in length), present in all three kingdoms, and long versions (750–930 amino acids), present only in eukaryotes. The recently solved crystal structure of the bacterial tRNase Z provides the structural basis for the understanding of central functional elements. The substrate is recognized by an exosite that protrudes from the main protein body and consists of a metallo-β-lactamase domain. Cleavage of the precursor tRNA occurs at the binuclear zinc site located in the other subunit of the functional homodimer. The first gene of the tRNase Z family was cloned in 2002. Since then a comprehensive set of data has been acquired concerning this new enzyme, including detailed functional studies on purified recombinant enzymes, mutagenesis studies and finally the determination of the crystal structure of three bacterial enzymes. This review summarizes the current knowledge about these exciting enzymes.

Keywords: elaC; metallo-β-lactamases; RNase BN; tRNA processing; tRNase Z; ZiPD

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Published Online: 2005-12-09

Published in Print: 2005-12-01


Citation Information: Biological Chemistry, Volume 386, Issue 12, Pages 1253–1264, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.142.

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