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A splice variant of the human CCA-adding enzyme with modified activity
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology.ORCID iD: 0000-0002-4383-9880
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2007 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 366, no 4, 1258-1265 p.Article in journal (Refereed) Published
Abstract [en]

The human CCA-adding enzyme (tRNA nucleotidyltransferase) is an essential enzyme that catalyzes the addition of the CCA terminus to the 3′ end of tRNA precursors, a reaction which is a fundamental prerequisite for mature tRNAs to become aminoacylated and to participate in protein biosynthesis. To date only one form of this enzyme has been identified in humans. Here, we describe the sequence and activity of a splice variant of the human CCA-adding enzyme identified in public cDNA databases. The in silico analyses performed on this splice variant indicate that there is conservation of the alternative splice donor site among species and indicate that it seems to be used in vivo. Moreover, the recombinantly expressed protein is active in vitro and accepts tRNA transcripts as substrates incorporating the dinucleotide sequence CC to their 3′ end, in contrast to the activity of the full length enzyme. These findings strongly suggest that the splice variant of the human CCA-adding enzyme is expressed in the cell although the in vivo function remains unclear.

Place, publisher, year, edition, pages
2007. Vol. 366, no 4, 1258-1265 p.
Keyword [en]
alternative splicing, CC-adding enzyme, CCA-adding enzyme, tRNA nucleotidyltransferase
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-11074DOI: 10.1016/j.jmb.2006.12.016ISI: 000244649500017PubMedID: 17204286OAI: oai:DiVA.org:uu-11074DiVA: diva2:38842
Available from: 2007-05-22 Created: 2007-05-22 Last updated: 2017-12-11Bibliographically approved

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Schuster, Jens

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