Journal
PROTEIN AND PEPTIDE LETTERS
Volume 14, Issue 2, Pages 137-145Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986607779816050
Keywords
3'-tRNase; RNase Z; tRNA 3' endonuclease; metallo-beta-lactamase domain; tRNA processing; tRNase; Trz
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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.
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