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Published online before print June 2, 2006, 10.1110/ps.062197206
Protein Science (2006), 15:1791-1793. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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FOR THE RECORD

Dissociation of intermolecular disulfide bonds in P22 tailspike protein intermediates in the presence of SDS

Junghwa Kim and Anne Skaja Robinson

Department of Chemical Engineering, University of Delaware, Newark, Delaware 19716, USA

(RECEIVED March 2, 2006; FINAL REVISION April 10, 2006; ACCEPTED April 10, 2006)

Each chain of the native trimeric P22 tailspike protein has eight cysteines that are reduced and buried in its hydrophobic core. However, disulfide bonds have been observed in the folding pathway and they are believed to play a critical role in the registration of the three chains. Interestingly, in the presence of sodium dodecyl sulfate (SDS) only monomeric chains, rather than disulfide-linked oligomers, have been observed from a mixture of folding intermediates. Here we show that when the oligomeric folding intermediates were separated from the monomer by native gel electrophoresis, the reduction of intermolecular disulfide bonds did not occur in the subsequent second-dimension SDS–gel electrophoresis. This result suggests that when tailspike monomer is present in free solution with SDS, the partially unfolded tailspike monomer can facilitate the reduction of disulfide bonds in the tailspike oligomers.

Keywords: P22 tailspike protein (TSP); transient disulfide bond; assembly; disulfide shuffling; SDS


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