Primer protein of bacteriophage M2 exposes the RGD receptor site upon linking the first deoxynucleotide.
Primer protein (PP) of bacteriophages M2 and phi 29 contains an Arg-Gly-Asp (RGD) sequence. The RGD-mediated protein-protein interaction in protein-primed DNA replication of M2 was studied in vitro using three purified and indispensable components: PP, DNA polymerase (POL) and template DNA linked to terminal protein (TP). PP competed with a synthetic RGD peptide for binding to the template DNA-TP complex (TP-DNA). In addition, POL bound to template TP-DNA only when complexed with PP. These results indicate that the RGD sequence of PP is responsible for the interaction of the PP-POL complex with TP-DNA, which contains the initiation site for the protein priming of DNA synthesis. At the moment when PP converts to TP upon linking the first deoxynucleotide, a conformational change results in exposure of the RGD binding site.
Kobayashi
H
H
Life Science Institute, Sophia University, Tokyo, Japan.
Kitabayashi
K
K
Matsumoto
K
K
Hirokawa
H
H
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000378:metabolism*; D001483:Base Sequence; D004247:DNA; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D003854:Deoxyribonucleotides / Q000378:metabolism*; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D013698:Templates, Genetic; D014764:Viral Proteins / Q000378:metabolism*
D004279:DNA, Viral; D003854:Deoxyribonucleotides; D009842:Oligopeptides; D014764:Viral Proteins; C068917:primer protein, Bacteriophage M2; C047981:arginyl-glycyl-aspartic acid; D004247:DNA; D004259:DNA-Directed DNA Polymerase