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J Biol Chem, Vol. 274, Issue 23, 16141-16146, June 4, 1999

Folding and Stability of Mutant Scaffolding Proteins Defective in P22 Capsid Assembly

From the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Bacteriophage P22 scaffolding subunits are elongated molecules that interact through their C termini with coat subunits to direct icosahedral capsid assembly. The soluble state of the subunit exhibits a partially folded intermediate during equilibrium unfolding experiments, whose C-terminal domain is unfolded (Greene, B., and King, J. (1999) J. Biol. Chem. 274, 16135-16140). Four mutant scaffolding proteins exhibiting temperature-sensitive defects in different stages of particle assembly were purified. The purified mutant proteins adopted a similar conformation to wild type, but all were destabilized with respect to wild type. Analysis of the thermal melting transitions showed that the mutants S242F and Y214W further destabilized the C-terminal domain, whereas substitutions near the N terminus either destabilized a different domain or affected interactions between domains. Two mutant proteins carried an additional cysteine residue, which formed disulfide cross-links but did not affect the denaturation transition. These mutants differed both from temperature-sensitive folding mutants found in other P22 structural proteins and from the thermolabile temperature-sensitive mutants described for T4 lysozyme. The results suggest that the defects in these mutants are due to destabilization of domains affecting the weak subunit-subunit interactions important in the assembly and function of the virus precursor shell.

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				P. A. Thuman-Commike, B. Greene, J. Jakana, A. McGough, P. E. Prevelige, and W. Chiu Identification of Additional Coat-Scaffolding Interactions in a Bacteriophage P22 Mutant Defective in Maturation J. Virol., April 15, 2000; 74(8): 3871 - 3873. [Abstract] [Full Text]

				B. Greene and J. King In Vitro Unfolding/Refolding of Wild Type Phage P22 Scaffolding Protein Reveals Capsid-binding Domain J. Biol. Chem., June 4, 1999; 274(23): 16135 - 16140. [Abstract] [Full Text] [PDF]