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

BMC Biochemistry
Gopinath MuruganandamPetri Kursula

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). We employed different biophysical and biochemical methods to elucidate the overall structural and functional features of the tRNA healing enzymes yeast Trl1 PNK/CPDase and lancelet PNK/CPDase and compared them with vertebrate CNPase. The yeast and the lancelet enzymes have cyclic phosphodiesterase and polynucleotide kinase activity, while vertebrate CNPase lacks PNK activity. In addition, we also show that the healing enzymes are structurally similar to the vertebrate CNPase by applying synchrotron radiation circular dichroism spectroscopy and small-angle X-ray scattering. We provide a structural analysis of the tRNA healing enzyme PNK and CPDase doma...Continue Reading

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Citations

Sep 1, 2018·Protein Science : a Publication of the Protein Society·Andrew J Miles, B A Wallace

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Methods Mentioned

BETA
phosphotransferase
phosphotransferases
PCR
size exclusion chromatography
circular dichroism
electrophoresis
thermal shift
X-ray
pulldown
NMR

Software Mentioned

Protein Crystallographic Construct Design ( ProteinCCD ) metas...
CDtool
ATSAS
MONSA
DAMMIF
GASBOR
Dichroweb
iControl
GNOM

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