Characterization and mapping of the pyrophosphorolytic activity of the phage phi 29 DNA polymerase. Involvement of amino acid motifs highly conserved in alpha-like DNA polymerases.-Reference-Cited by-同舟云学术

Characterization and mapping of the pyrophosphorolytic activity of the phage phi 29 DNA polymerase. Involvement of amino acid motifs highly conserved in alpha-like DNA polymerases.

Published:1991-04 Issue:12 Volume:266 Page:7904-7909
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Blasco M A,Bernad A,Blanco L,Salas M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference29 articles.

1. Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases.

2. A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases

3. The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization.

4. Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication.

5. Replication of phage phi 29 DNA with purified terminal protein and DNA polymerase: synthesis of full-length phi 29 DNA.

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