Purification and properties of bacteriophage phi X 174 gene D product.
Bacteriophage phi X 174 gene D product, a protein required for single-stranded DNA synthesis by the phage, has been purified to near homogeneity. The protein is very abundant; approximately 10(5) monomers are present per infected cell when lysis is delayed. The protein has a monomer molecular weight of 15,200 and is normally a tetramer; however, it can form very large aggregates at high concentrations. Amino acid analysis shows an excess of arginine over lysine and a relatively high number of nonpolar residues. The protein carries a net negative charge at neutral pH. The first eight amino acids of the protein sequence have been determined; they are Ser-Gln-Val-Thr-Glu-Gln-Arg-Val. The carboxy-terminal residue is methionine. The protein has not yet been shown to bind directly to any single-stranded DNA; it does not adsorb to denatured calf thymus DNA-cellulose.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001120:Arginine / Q000032:analysis; D003090:Coliphages / Q000032:analysis* / Q000378:metabolism; D004267:DNA Viruses; D004277:DNA, Single-Stranded / Q000096:biosynthesis / Q000378:metabolism; D004279:DNA, Viral / Q000096:biosynthesis / Q000378:metabolism; D005796:Genes; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D011485:Protein Binding; D014176:Protein Biosynthesis; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism
D000596:Amino Acids; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D010455:Peptides; D014764:Viral Proteins; D001120:Arginine