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RNA uridylyltransferases

RNA uridylyltransferases .The terminal RNA uridylyltransferases (TUTases) catalyze transfer of UMP residues to the 3′ hydroxyl group of RNA. These activities are widespread among eukaryotes and appear to be involved in a variety of RNA-processing pathways. Recent studies of RNA editing in trypanosomatids have provided the first insights into the biological functions of RNA uridylyltransferases, which had eluded biochemical identification despite 30-year-old evidence of such activities in mammals and plants. Comparative sequence analysis of trypanosomal TUTases and their homologs revealed by large-scale genomic projects demonstrates a significant level of biochemical and structural diversity between putative uridylyltransferases. The conserved catalytic domain has acquired additional protein modules and appears to have adapted to perform functionally distinct tasks of guided U-insertion into mRNA and constrained addition of an oligo[U] tail to guide RNAs. Here I discuss the current knowledge of this novel enzyme family and possible roles of RNA uridylylation in the regulation of gene expression. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular and Molecular Life Sciences Springer Journals

RNA uridylyltransferases

Cellular and Molecular Life Sciences , Volume 62 (19-20) – Oct 1, 2005

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References (85)

Publisher
Springer Journals
Copyright
Copyright © Birkhäuser Verlag, Basel 2005
Subject
Life Sciences; Life Sciences, general; Biomedicine general; Biochemistry, general; Cell Biology
ISSN
1420-682X
eISSN
1420-9071
DOI
10.1007/s00018-005-5198-9
pmid
16158189
Publisher site
See Article on Publisher Site

Abstract

.The terminal RNA uridylyltransferases (TUTases) catalyze transfer of UMP residues to the 3′ hydroxyl group of RNA. These activities are widespread among eukaryotes and appear to be involved in a variety of RNA-processing pathways. Recent studies of RNA editing in trypanosomatids have provided the first insights into the biological functions of RNA uridylyltransferases, which had eluded biochemical identification despite 30-year-old evidence of such activities in mammals and plants. Comparative sequence analysis of trypanosomal TUTases and their homologs revealed by large-scale genomic projects demonstrates a significant level of biochemical and structural diversity between putative uridylyltransferases. The conserved catalytic domain has acquired additional protein modules and appears to have adapted to perform functionally distinct tasks of guided U-insertion into mRNA and constrained addition of an oligo[U] tail to guide RNAs. Here I discuss the current knowledge of this novel enzyme family and possible roles of RNA uridylylation in the regulation of gene expression.

Journal

Cellular and Molecular Life SciencesSpringer Journals

Published: Oct 1, 2005

Keywords: Uridylyltransferase; TUTase; RNA editing; editosome; Trypanosoma; Leishmania; gRNA; U6 snRNP; cytoplasmic poly(A) polymerase

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