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tRNase Z

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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. Z.





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

Document Type: Research Article

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

Publication date: February 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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