Abstract
It is shown that gene 5 protein of bacteriophage M13 is one of the major proteins synthesized in vitro under the direction of M13 replicative-form DNA. By means of DNA-cellulose chromatography, this protein has been purified to homogeneity and its biological characteristics have been compared with those of its native counterpart. Like native gene 5 protein, the purified, in vitro-synthesized protein binds tightly and selectively to single-stranded, but not to double-stranded, DNAs. These results suggest that truly functional gene 5 protein is made in the cell-free system.
MeSH Terms
Autoradiography
Carbon Radioisotopes
Cell-Free System
Chromatography, DEAE-Cellulose
Coliphages/analysis,metabolism
DNA, Single-Stranded/metabolism
DNA, Viral/isolation & purification,metabolism
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Genes
Leucine/metabolism
Protein Binding
Sulfur Radioisotopes
Viral Proteins/analysis,biosynthesis,isolation & purification,metabolism
Chemicals
Carbon Radioisotopes
DNA, Single-Stranded
DNA, Viral
Sulfur Radioisotopes
Viral Proteins
Leucine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Konings R N
Jansen J
Cuypers T
Schoenmakers J G
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27 references, click to expand
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