Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.

Muruganandam, Gopinath; Raasakka, Arne; Myllykoski, Matti; Kursula, Inari; Kursula, Petri

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Authors

Muruganandam, Gopinath
Raasakka, Arne
Myllykoski, Matti
Kursula, Inari
Kursula, Petri

Issue Date

2017-05-16

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Abstract

Eukaryotic tRNA splicing is an essential process in the transformation of a primary tRNA transcript into a mature functional tRNA molecule. 5'-phosphate ligation involves two steps: a healing reaction catalyzed by polynucleotide kinase (PNK) in association with cyclic phosphodiesterase (CPDase), and a sealing reaction catalyzed by an RNA ligase. The enzymes that catalyze tRNA healing in yeast and higher eukaryotes are homologous to the members of the 2H phosphoesterase superfamily, in particular to the vertebrate myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase).

Citation

Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase. 2017, 18 (1):7 BMC Biochem.

Affiliation

Helmholtz Centre for infection research, Inhoffenstr.7, 38124 Braunschweig, Germany.

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Article

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ISSN

1471-2091

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publications of the scientific administration (GFW)

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Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/