Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase

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Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	153593
Author(s)	Wahle, E.; Martin, G.; Schiltz, E.; Keller, W.
Author(s) at UniBasel	Keller, Walter
Year	1991
Title	Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase
Journal	The EMBO Journal
Volume	10
Number	13
Pages / Article-Number	4251-7
Keywords	Amino Acid Sequence; Animals; Base Sequence; Blotting; Northern; Cattle; Chromatography; Liquid; Cloning; Molecular; DNA/genetics/isolation & purification; Electrophoresis; Polyacrylamide Gel; Escherichia coli/genetics; Gene Expression; Genes; Bacterial; Hela Cells; Humans; Molecular Sequence Data; Plasmids; Polymerase Chain Reaction; Polynucleotide Adenylyltransferase/genetics; RNA; Messenger/metabolism
Abstract	cDNA clones encoding mammalian poly(A) polymerase were isolated with probes generated by the polymerase chain reaction based on amino acid sequences derived from the purified enzyme. A bovine cDNA clone was obtained encoding a protein of 82 kDa. Expression in Escherichia coli resulted in the appearance of a poly(A) polymerase activity that was dependent on the addition of the purified specificity factor CPF and the presence of the polyadenylation signal AAUAAA in the RNA substrate. The activity copurified with a polypeptide of the expected size. A second class of cDNAs encoded a polypeptide of 43 kDa which was closely related to the N-terminal half of the 82 kDa protein. Northern blots showed two mRNAs of 4.2 and 2.4 kb that probably correspond to the two classes of cDNAs, as well as a third band of 1.3 kb. The sequence of the N-terminal half of bovine poly(A) polymerase is 47% identical with the amino acid sequence of the corresponding part of yeast poly(A) polymerase. Homologies to other proteins are of uncertain significance.
Publisher	Nature Publishing Group
ISSN/ISBN	0261-4189 ; 1460-2075
URL	http://onlinelibrary.wiley.com/doi/10.1002/j.1460-2075.1991.tb05003.x/pdf
edoc-URL	http://edoc.unibas.ch/dok/A5257991
Full Text on edoc	No
PubMed ID	http://www.ncbi.nlm.nih.gov/pubmed/1756732
Document type (ISI)	Journal Article

03/05/2024

Research Database / FORSCHUNGSDATENBANK