Functional domains in the bacteriophage phi 29 terminal protein for interaction with the phi 29 DNA polymerase and with DNA.
Deletion mutants at the amino- and carboxyl-ends of the phi 29 terminal protein, as well as internal deletion and substitution mutants, whose ability to prime the initiation of phi 29 DNA replication was affected to different extent, have been assayed for their capacity to interact with DNA or with the phi 29 DNA polymerase. One DNA binding domain at the amino end of the terminal protein has been mapped. Two regions involved in the binding to the DNA polymerase, an internal region near the amino-terminus and a carboxyl-terminal one, have been also identified. Interaction with both DNA and phi 29 DNA polymerase are required to led to the formation of terminal protein-dAMP initiation complex to start phi 29 DNA replication.
Zaballos
A
A
Centro de Biologia Molecular (CSIC-UAM), Universidad Autónoma, Canto Blanco, Madrid, Spain.
Salas
M
M
D001435:Bacteriophages / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D003838:Deoxyadenine Nucleotides / Q000378:metabolism; D009154:Mutation; D009690:Nucleic Acid Conformation; D010957:Plasmids; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D004279:DNA, Viral; D003838:Deoxyadenine Nucleotides; D014764:Viral Proteins; C040784:terminal protein, Bacillus phage phi29; C012873:2'-deoxy-5'-adenosine monophosphate; D004259:DNA-Directed DNA Polymerase