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

2.50
Hdl Handle:
http://hdl.handle.net/10033/620972
Title:
Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.
Authors:
Muruganandam, Gopinath; Raasakka, Arne; Myllykoski, Matti; Kursula, Inari; Kursula, Petri
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).
Affiliation:
Helmholtz Centre for infection research, Inhoffenstr.7, 38124 Braunschweig, Germany.
Citation:
Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase. 2017, 18 (1):7 BMC Biochem.
Journal:
BMC biochemistry
Issue Date:
16-May-2017
URI:
http://hdl.handle.net/10033/620972
DOI:
10.1186/s12858-017-0084-2
PubMed ID:
28511668
Type:
Article
Language:
en
ISSN:
1471-2091
Appears in Collections:
publications of the scientific administration (GFW)

Full metadata record

DC FieldValue Language
dc.contributor.authorMuruganandam, Gopinathen
dc.contributor.authorRaasakka, Arneen
dc.contributor.authorMyllykoski, Mattien
dc.contributor.authorKursula, Inarien
dc.contributor.authorKursula, Petrien
dc.date.accessioned2017-06-21T14:46:09Z-
dc.date.available2017-06-21T14:46:09Z-
dc.date.issued2017-05-16-
dc.identifier.citationStructural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase. 2017, 18 (1):7 BMC Biochem.en
dc.identifier.issn1471-2091-
dc.identifier.pmid28511668-
dc.identifier.doi10.1186/s12858-017-0084-2-
dc.identifier.urihttp://hdl.handle.net/10033/620972-
dc.description.abstractEukaryotic 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).en
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleStructural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr.7, 38124 Braunschweig, Germany.en
dc.identifier.journalBMC biochemistryen
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