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PMID: 8665867 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases.

The EMBO journal ·Vol. 15 ·No. 10 ·1996-05-15 ·Pages 2593-603

Martin G, Keller W

Abstract

We have tested deletion and substitution mutants of bovine poly(A) polymerase, and have identified a small region that overlaps with a nuclear localization signal and binds to the RNA primer. Systematic mutagenesis of carboxylic amino acids led to the identification of three aspartates that are essential for catalysis. Sequence and secondary structure comparisons of regions surrounding these aspartates with sequences of other polymerases revealed a significant homology to the palm structure of DNA polymerase beta, terminal deoxynucleotidyltransferase and DNA polymerase IV of Saccharomyces cerevisiae, all members of the family X of polymerases. This homology extends as far as cca: tRNA nucleotidyltransferase and streptomycin adenylyltransferase, an antibiotic resistance factor.

MeSH Terms
Amino Acid Sequence Animals Aspartic Acid Binding Sites Caenorhabditis elegans/enzymology Cattle DNA Nucleotidylexotransferase/chemistry DNA Polymerase I/chemistry DNA Polymerase beta DNA-Directed DNA Polymerase/chemistry Fungal Proteins/chemistry Helminth Proteins/chemistry Humans Mice Models, Molecular Molecular Sequence Data Multigene Family Mutagenesis, Site-Directed Nucleotidyltransferases/chemistry,classification Polynucleotide Adenylyltransferase/chemistry,genetics,metabolism Protein Binding RNA/metabolism RNA Precursors/metabolism Recombinant Proteins/metabolism Saccharomyces cerevisiae/enzymology Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Deletion Sequence Homology, Amino Acid Species Specificity Xenopus laevis
Chemicals
Fungal Proteins Helminth Proteins RNA Precursors RNA primers Recombinant Proteins Saccharomyces cerevisiae Proteins Aspartic Acid RNA Nucleotidyltransferases Polynucleotide Adenylyltransferase DNA Nucleotidylexotransferase DNA Polymerase I DNA Polymerase beta DNA-Directed DNA Polymerase POL4 protein, S cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Martin G
Department of Cell Biology, University of Basel, Basel, Switzerland.
Keller W
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1996-05-15
Pages
2593-603
Language
English
Region
England
NLM ID
8208664
PMCID
PMC450192
Subset
IM
Databases
GENBANK
L22658, U19974, U19975, X76770
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