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. 1992 Oct 30;71(3):479-88.
doi: 10.1016/0092-8674(92)90516-f.

The reovirus cell attachment protein possesses two independently active trimerization domains: basis of dominant negative effects

G Leone  1 , L Maybaum, P W Lee
Affiliations

The reovirus cell attachment protein possesses two independently active trimerization domains: basis of dominant negative effects

G Leone et al. Cell. .

Abstract

The reovirus cell attachment protein, sigma 1, is a homotrimer with an N-terminal fibrous tail and a C-terminal globular head. By cotranslating full-length and various truncated sigma 1 proteins in vitro, we show that the N- and C-terminal halves of sigma 1 possess independent trimerization and folding domains. Trimerization of sigma 1 is initiated at the N-terminus by the formation of a "loose," protease-sensitive, three-stranded, alpha-helical coiled coil. This serves to bring the three unfolded C-termini into close proximity to one another, facilitating their subsequent trimerization and cooperative folding. Concomitant with, but independent of, this latter process, the N-terminal fiber further matures into a more stable and protease-resistant structure. The coordinated folding of sigma 1 trimers exemplifies the dominant negative effects of mutant subunits in oligomeric complexes.

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