ø29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 278 (4) , 741-755
- https://doi.org/10.1006/jmbi.1998.1724
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesPublished by Elsevier ,2004
- Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69Cell, 1997
- Crystal structure of a thermostable Bacillus DNA polymerase l large fragment at 2.1 Å resolutionStructure, 1997
- Activation of Replication Origins in ϕ29-related Phages Requires the Recognition of Initiation Proteins to Specific Nucleoprotein ComplexesJournal of Biological Chemistry, 1996
- Structural and Functional Organization of the DNA Polymerase of Bacteriophage T7Published by Elsevier ,1996
- Crystal Structures of an NH2-Terminal Fragment of T4 DNA Polymerase and Its Complexes with Single-Stranded DNA and with Divalent Metal IonsBiochemistry, 1996
- Primer Terminus Stabilization at the φ29 DNA Polymerase Active SitePublished by Elsevier ,1995
- Evidence favouring the hypothesis of a conserved 3′–5′ exonuclease active site in DNA-dependent DNA polymerasesGene, 1992
- Use of bacteriophage T7 lysozyme to improve an inducible T7 expression systemJournal of Molecular Biology, 1991
- An attempt to unify the structure of polymerasesProtein Engineering, Design and Selection, 1990