Residues in two homology blocks on the amino side of the tRNase Z His domain contribute unexpectedly to pre-tRNA 3' end processing.

RNA
Neela ZareenLouis Levinger

Abstract

tRNase Z, which can endonucleolytically remove pre-tRNA 3'-end trailers, possesses the signature His domain (HxHxDH; Motif II) of the beta-lactamase family of metal-dependent hydrolases. Motif II combines with Motifs III-V on its carboxy side to coordinate two divalent metal ions, constituting the catalytic core. The PxKxRN loop and Motif I on the amino side of Motif II have been suggested to modulate tRNase Z activity, including the anti-determinant effect of CCA in mature tRNA. Ala walks through these two homology blocks reveal residues in which the substitutions unexpectedly reduce catalytic efficiency. While substitutions in Motif II can drastically affect k(cat) without affecting k(M), five- to 15-fold increases in k(M) are observed with substitutions in several conserved residues in the PxKxRN loop and Motif I. These increases in k(M) suggest a model for substrate binding. Expressed tRNase Z processes mature tRNA with CCA at the 3' end approximately 80 times less efficiently than a pre-tRNA possessing natural sequence of the 3'-end trailer, due to reduced k(cat) with no effect on k(M), showing the CCA anti-determinant to be a characteristic of this enzyme.

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Citations

Apr 12, 2007·Nucleic Acids Research·Lisa J SchererJohn J Rossi
Jul 28, 2007·Biochemistry·Shay KarkashonLouis Levinger
Apr 9, 2009·The Journal of Biological Chemistry·Louis LevingerChristopher Wilson
Apr 16, 2009·The Journal of Biological Chemistry·Tanmay Dutta, Murray P Deutscher
Apr 25, 2007·Critical Reviews in Biochemistry and Molecular Biology·Zbigniew Dominski
Oct 1, 2008·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Hiroaki Takaku, Masayuki Nashimoto
Apr 6, 2017·Nucleic Acids Research·Miao MaHerman van Tilbeurgh
Aug 3, 2021·Disease Models & Mechanisms·Ekaterina MigunovaEdward B Dubrovsky

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