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. 1983 Dec;80(23):7060–7064. doi: 10.1073/pnas.80.23.7060

Genetic analysis of the folding pathway for the tail spike protein of phage P22.

D P Goldenberg, D H Smith, J King
PMCID: PMC389992  PMID: 6227917

Abstract

Temperature-sensitive mutations in the gene encoding the trimeric tail spike protein of phage P22 interfere with protein maturation at 39 degrees C. We show here that temperature-sensitive mutations at many sites block the folding pathway prior to accumulation of the partially folded protrimer intermediate. Temperature-shift experiments indicate that at least some of the mutants accumulate an earlier intermediate in the folding pathway. Immunoprecipitation experiments suggest that the conformation of the isolated temperature-sensitive polypeptide chains is closer to that of the unfolded chain than to that of the mature spike formed at permissive temperature. The sites of these mutations probably represent amino acid sequences that play key roles during the folding of the tail spike polypeptide chain but are not important in the mature protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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