tRNase Z

Maria      Ceballos; Agustin      Vioque

Abstract

Endonuclease tRNase Z catalyzes the generation of the mature 3 end of tRNA precursors through specific endonucleolytic cleavage. The enzyme has been characterized from organisms representative of all domains of life as well as from organelles, and the crystal structure of three bacterial enzymes has been determined. This review presents an overview of its properties and what is known about its structure, substrate recognition, cleavage site definition, and potential practical applications. Z.

Keywords: 3'-tRNase, RNase Z, tRNA 3' endonuclease, metallo-β -lactamase domain, tRNA processing, tRNase, Trz

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Protein & Peptide Letters

Title: tRNase Z

Volume: 14 Issue: 2

Author(s): Maria Ceballos and Agustin Vioque

Affiliation:

Keywords: 3'-tRNase, RNase Z, tRNA 3' endonuclease, metallo-β -lactamase domain, tRNA processing, tRNase, Trz

Abstract: Endonuclease tRNase Z catalyzes the generation of the mature 3 end of tRNA precursors through specific endonucleolytic cleavage. The enzyme has been characterized from organisms representative of all domains of life as well as from organelles, and the crystal structure of three bacterial enzymes has been determined. This review presents an overview of its properties and what is known about its structure, substrate recognition, cleavage site definition, and potential practical applications. Z.