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Nonnative Interactions between Cysteines Direct Productive Assembly of P22 Tailspike Protein

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

Correspondence: Address reprint requests to Anne Skaja Robinson, 259 Colburn Laboratory, Dept. of Chemical Engineering, University of Delaware, Newark, DE 19716 USA. Tel.: 302-831-0557; Fax: 302-831-6262; E-mail: robinson{at}che.udel.edu.

Nonnative disulfide bond formation can play a critical role in the assembly of disulfide bonded proteins. During the folding and assembly of the P22 tailspike protein, nonnative disulfide bonds form both in vivo and in vitro. However, the mechanism and identity of cysteine disulfide pairs remains elusive, particularly for P22 tailspike, which contains no disulfide bonds in its native, functional form. Understanding the interactions between cysteine residues is important for developing a mechanistic model for the role of nonnative cysteines in P22 tailspike assembly. Prior in vivo studies have suggested that cysteines 496, 613, and 635 are the most likely site for sulfhydryl reactivity. Here we demonstrate that these three cysteines are critical for efficient assembly of tailspike trimers, and that interactions between cysteine pairs lead to productive assembly of native tailspike.

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