Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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tRNase Z

Author(s): Maria Ceballos and Agustin Vioque

Affiliation: Instituto de Bioquimica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Americo Vespucio 49,41092 Sevilla, Spain.

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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Article Details

VOLUME: 14
ISSUE: 2
Page: [137 - 145]
Pages: 9
DOI: 10.2174/092986607779816050
Price: $58