Phi29 polymerase structure
Web13. jún 2024 · Phi29 DNA polymerase, derived from Bacillus subtilis phage phi29, is widely used for DNA amplification through rolling-circle replication or multiple displacement amplification ( Dean et al., 2001; Dean et al., 2002) because of its high processivity ( Blanco et al., 1989 ), a strand displacement activity, high fidelity ( Esteban et al., 1993) and … Web25. júl 2007 · To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymerases, complexed with primer-template DNA in the presence or absence of the incoming nucleoside triphosphate, the pre- and post-translocated states, respectively.
Phi29 polymerase structure
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Web22. mar 2006 · The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition The absolute requirement for primers in the initiation of DNA synthesis poses a problem for replicating the ends of linear chromosomes. Web15. mar 2002 · The most recent members of the crystallographic database from the DNA pol I group (family A) are the DNA polymerase structures of Thermus aquaticus , bacteriophage T7 and ... Relating structure to function in phi29 DNA polymerase. J. Biol. Chem., 271, 8509 –8512. 13. Salas,M.
WebBacteriophage Phi29 DNA polymerase belongs to the protein-primed subgroup of family B DNA polymerases that use a terminal protein (TP) as a primer to initiate genome replication. The resolution of the crystallographic structure showed that it consists of an N-terminal domain with the exonuclease activity and a C-terminal polymerization domain. Webstructure summary. Φ29 DNA polymerase is an enzyme from the bacteriophage Φ29. It is being increasingly used in molecular biology for multiple displacement DNA amplification procedures, and has a number of features that make …
WebInitial structural studies provided insights into the intrinsic strand displacement, processivity, and protein priming activ-ities of phi29 DNAP. The structure of the apo phi29 DNAP exhibited two globular domains, an N-terminal exonuclease domain and a C-terminal polymerase domain. This structure contains three tunnels, one of which is formed ... Web29. nov 2015 · Unlike animals, sRNA constructs have provenvery effective inducinggene silencing plants.Here, we described noveltechnique based generatingmultiple lhRNA constructs indi-vidual gene cDNAs.Phi29 DNA polymerase RCA-mediatedhpRNA (RMHR) construction system because itscapacity performstrand displacement DNA synthesis …
Web29. sep 2024 · Phage phi29 protein p5 is the SSB protein active during phi29 DNA replication. It protects ssDNA against nuclease degradation and greatly stimulates dNTP incorporation during phi29 DNA replication process. Binding of the SSB to ssDNA prevents non-productive binding of the viral DNA polymerase to ssDNA, and allows the release …
Web29. jan 2024 · ϕ29 DNA polymerase is the only member of the protein-primed subgroup of DNA polymerases whose structure has been solved. It has a N-terminal domain (residues 1–189) with the 3′-5′ exonuclease... oregon dhs medical release formWebNon-enveloped, head-tail structure. The prolate capsid is about 45 x 54 nm, with a T=3, Q=5 symmetry . The tail is non-contractile and has a collar with 12 appendages attached to the neck region that are important for host cell recognition and entry. The 55 capsid (head) fibers are not always present and may have been lost in some lab strains. oregon dhs foundations trainingWeb7. sep 2010 · Bacteriophage φ29 DNA polymerase is a unique enzyme endowed with two distinctive properties, high processivity and faithful polymerization coupled to strand displacement, that have led to the development of protocols to achieve isothermal amplification of limiting amounts of both circular plasmids and genomic DNA. how to unhide columns a in excelWeb5. feb 1992 · Based on these data, the phi 29 DNA polymerase, a model enzyme for protein-primed DNA replication, appears to share the same mechanism for the editing function as that first proposed for T4 DNA polymerase and Escherichia coli DNA polymerase I on the basis of functional and structural studies. Publication types Research Support, Non-U.S. … oregon dhs forms pageWeb16. máj 2007 · Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex) PDB DOI: 10.2210/pdb2PYL/pdb NDB: PD1012 Classification: REPLICATION, TRANSFERASE/DNA Organism (s): Salasvirus phi29 Expression System: Escherichia coli Mutation (s): Yes Deposited: 2007-05-16 Released: … how to unhide columns a-c in excelWeb11. apr 2024 · The Phi29 DNA polymerase we used was a previously reported mutant with an optimum activity at temperatures of 40℃–60°C (Fig. 3 D) [33]. To determine whether the light control of DNA polymerase can address the limitation of inconsistent amplification initiation in RCA, we performed quantitative RCA reactions to detect plasmid DNA using … how to unhide columns and rows in excelWeb1. apr 2002 · The results suggest that Lys371 of phi29 DNA polymerase, highly conserved among families A and B, interacts with the phosphate groups of the incoming nucleotide. On the other hand, the role of residue Ile364 seems to be structural, being important for both DNA and dNTP binding. oregon dhs government relations