Site-directed mutagenesis of the YCDTDS amino acid motif of the phi 29 DNA polymerase

Gene
A BernadM Salas

Abstract

The Bacillus subtilis phage phi 29 DNA polymerase, involved in protein-primed viral DNA replication, contains amino acid consensus sequences common to other alpha-like DNA polymerases. Using site-directed mutagenesis we have studied the functional significance of the most conserved C-terminal segment mainly represented by the YCDTDS motif. A series of single point mutants has been constructed and the corresponding proteins have been overproduced and characterized. Measurements, on crude fractions, of the activity of the mutant proteins in the formation of the protein p3-dAMP initiation complex and in an in situ DNA polymerase assay, indicate that the YCDTDS domain is involved both in initiation and in elongation reactions.

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Citations

Feb 22, 2012·Biochemistry·Robert J BauerMichael A Trakselis
May 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·Q Li, F E Nargang
Apr 7, 2004·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Thomas A Steitz, Y Whitney Yin
Aug 8, 2008·Biology Direct·Igor B RogozinEugene V Koonin
Sep 18, 2013·Biochimica Et Biophysica Acta·Samuel L C MoorsArnout Ceulemans

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