Abstract
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.
MeSH Terms
Amino Acid Sequence
Amino Acids/analysis
Arginine/analysis
Coliphages/analysis,metabolism
DNA Viruses
DNA, Single-Stranded/biosynthesis,metabolism
DNA, Viral/biosynthesis,metabolism
Genes
Molecular Weight
Peptides/analysis
Protein Binding
Protein Biosynthesis
Viral Proteins/analysis,isolation & purification,metabolism
Chemicals
Amino Acids
DNA, Single-Stranded
DNA, Viral
Peptides
Viral Proteins
Arginine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Farber M B
References (32)
32 references, click to expand
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