Jun 24, 2004

P22 tailspike trimer assembly is governed by interchain redox associations

Biochimica Et Biophysica Acta
Brenda L Danek, A Robinson

Abstract

Though disulfide bonds are absent from P22 tailspike protein in its native state, a disulfide-bonded trimeric intermediate has been identified in the tailspike folding and assembly pathway in vitro. The formation of disulfide bonds is critical to efficient assembly of native trimers as mutations at C-terminal cysteines reduce or inhibit trimer formation. We investigated the effect of different redox folding environments on tailspike formation to discover if simple changes in reducing potential would facilitate trimer formation. Expression of tailspike in trxB cell lines with more oxidizing cytoplasms led to lower trimer yields; however, observed assembly rates were unchanged. In vitro, the presence of any redox buffer decreased the overall yield compared to non-redox buffered controls; however, the greatest yields of the native trimer were obtained in reducing rather than oxidizing environments at pH 7. Slightly faster trimer formation rates were observed in the redox samples at pH 7, perhaps by accelerating the reduction of the disulfide-bonded protrimer to the native trimer. These rates and the effects of the redox system were found to depend greatly on the pH of the refolding reaction. Oxidized glutathione (GSSG) trapped a t...Continue Reading

Mentioned in this Paper

Buffers
Biochemical Pathway
Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Glutathione Disulfide
Aggregation
Protein Structure, Quaternary
Sputolysin
Dithiothreitol
Tailspike protein, bacteriophage

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