Primer-terminus stabilization at the 3'-5' exonuclease active site of phi29 DNA polymerase. Involvement of two amino acid residues highly conserved in proofreading DNA polymerases.

Lignende værker

• Characterization of a 3'----5' exonuclease activity in the phage phi 29-encoded DNA polymerase.
  af: Blanco, L, et al.
  Udgivet: (1985)
• The Loop of the TPR1 Subdomain of Phi29 DNA Polymerase Plays a Pivotal Role in Primer-Terminus Stabilization at the Polymerization Active Site
  af: del Prado, Alicia, et al.
  Udgivet: (2019)
• Replication of phage phi 29 DNA with purified terminal protein and DNA polymerase: synthesis of full-length phi 29 DNA.
  af: Blanco, L, et al.
  Udgivet: (1985)
• Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases
  af: Berman, Andrea J, et al.
  Udgivet: (2007)
• Functional domains in the bacteriophage phi 29 terminal protein for interaction with the phi 29 DNA polymerase and with DNA.
  af: Zaballos, A, et al.
  Udgivet: (1989)