A RepA-like protein from bacteriophage BFK20 is a multifunctional protein with primase, polymerase, NTPase and helicase activities.

Phage BFK20 replication protein gp43 comprises an N-terminal prim-pol domain and a C-terminal domain similar to replicative helicases. We prepared and studied two recombinant proteins: gp43-1 containing both prim-pol and helicase domains, and gp43C with the helicase domain only. A SEC-MALS analysis indicated that gp43-1 forms a hexameric homooligomer.

Characterization of a phiBP endolysin encoded by the Paenibacillus polymyxa CCM 7400 phage.

Endolysin (gp1.2) from the Paenibacillus polymyxa CCM 7400 temperate phage phiBP has a modular structure consisting of an N-terminal region with a catalytic glycosyl hydrolase 25 domain and a C-terminal cell wall-binding domain. The entire gene of this endolysin and fragments containing its catalytic and binding domains separately were cloned into expression vectors and the corresponding recombinant proteins were expressed in Escherichia coli and purified by affinity chromatography.

Interaction between phage BFK20 helicase gp41 and its host Brevibacterium flavum primase DnaG.

Protein-protein interactions have been identified between the replication proteins of corynephage BFK20 and its host Brevibacterium flavum CCM 251. We tested the interactions between phage proteins gp40, gp41, gp42, gp43 and gp44 and between these phage proteins and host replication proteins DnaZX, DnaN, Dnaδ, DnaG, DnaA, RecF, TrxC, TrxB1 and SSB using a bacterial two-hybrid system. Phage proteins gp41, gp42 and gp43 self-associated, demonstrating that these proteins are oligomers in vivo.