Journal
MOLECULAR CELL
Volume 16, Issue 4, Pages 609-618Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2004.10.019
Keywords
-
Categories
Funding
- NIGMS NIH HHS [2R01 GM27242-24, R01 GM57510] Funding Source: Medline
Ask authors/readers for more resources
The DNA polymerase from phage Phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of Phi29 DNA polymerase determined at 2.2 Angstrom resolution provides explanations for its extraordinary processivity and strand displacement activities. Homology modeling suggests that downstream template DNA passes through a tunnel prior to entering the polymerase active site. This tunnel is too small to accommodate double-stranded DNA and requires the separation of template and non-template strands. Members of the B family of DNA polymerases that use protein primers contain two sequence insertions: one forms a domain not previously observed in polymerases, while the second resembles the specificity loop of T7 RNA polymerase. The high processivity of Phi29 DNA polymerase may be explained by its topological encirclement of both the downstream template and the upstream duplex DNA.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available