Structural and functional studies on ø29 DNA polymerase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics (clinical),Genetics
Link
http://link.springer.com/content/pdf/10.1007/BF02451783.pdf
Reference36 articles.
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2. Bernad A., Zaballos A., Salas M., Blanco L. (1987) Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases. EMBO J. 6:4219–4225
3. Bernad A., Blanco L., Lázaro J.M., Martin G., Salas M. (1989) A conserved 3′–5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases. Cell 59:219–228
4. Bernad A., Lázaro J.M., Salas M., Blanco L. (1990) The highly conserved amino acid sequence motifTyr-Gly-Asp-Thr-Asp-Ser in α-like DNA polymerases is required by phage ø29 DNA polymerase for protein-primed initiation and polymerization. Proc. Natl. Acad. Sci. USA 87:4610–4614
5. Blanco L., Salas M. (1984) Characterization and purification of a phage ø29-encoded DNA polymerase required for the initiation of replication. Proc. Natl. Acad. Sci. USA 81:5325–5329
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