Studies on phage internal proteins (original) (raw)

Virology, 1974

Abstract

Abstract Internal protein precursors (IP) are formed in Escherichia coli B cells, soon after infection with bacteriophage T4. These precursors are cleaved to internal protein products (IP∗) in E. coli B infected with a wild type of T4, but not after infection with an amber mutant defective in gene 21. It has been shown that T4 internal protein products (IP∗), formed either in vitro or in vivo , interact with T4 DNA, but not with the DNA of E. coli B, Clostridium perfringens , bacteriophage T2, lambda, or ∅X174. The specific binding of T4 internal proteins to T4 DNA is not due to glucose residues on phage DNA, since DNA preparations from a glucosyl transferase mutant (T4 am αgt am βgt ) or T4 DNA after digestion with β-glucosidase, retain their ability to bind T4 internal proteins. Internal protein precursors (IP) do not form detectable complexes with phage DNA. The proteins bound to T4 DNA in vitro , have been identified as internal proteins by polyacrylamide gel electrophoresis and have the respective molecular weights of 7600, 8600 and 18,000 d.

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