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J. Biol. Chem., Vol. 255, Issue 7, 2897-2901, 04, 1980

A temperature-sensitive single-stranded DNA-binding protein from Escherichia coli

RR Meyer, J Glassberg, JV Scott and A Kornberg

A temperature-sensitive single-stranded DNA-binding protein (SSB) has been purified from mutant Escherichia coli (ssb-1) cells by use of affinity chromatography on blue dextran-Sepharose. An altered amino acid sequence in the mutant protein is apparent in tryptic digests, confirming that the ssb mutation is in the structural gene. The mutant protein is less effective than the wild type in protecting single- stranded DNA from nuclease S1 digestion and in inhibiting DNA-dependent ATPases. The purified protein supports replication of phage G4 DNA in vitro at 30 degrees C, although higher levels of mutant protein, 4-fold higher than wild type, are needed to do so. The mutant protein becomes less active in supporting replication above 30 degrees C and becomes inactive at 42 degrees C within 1 min. Activity is restored upon return to 20 degrees C. Despite its temperature sensitivity in vivo and in vitro, the mutant binding protein can renature fully after exposure to 100 degrees C. Thus, the mutant protein is both heat-stable and functionally temperature-sensitive.
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