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PMID: 1255852 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Purification and properties of bacteriophage phi X 174 gene D product.

Journal of virology ·Vol. 17 ·No. 3 ·1976-03-00 ·Pages 1027-37

Farber MB

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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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1976-03-00
Pages
1027-37
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC515501
Subset
IM
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