The reovirus cell attachment protein possesses two independently active trimerization domains: basis of dominant negative effects. Cell 1992 Oct 30;71(3):479-88
Date
10/30/1992Pubmed ID
1423608DOI
10.1016/0092-8674(92)90516-fScopus ID
2-s2.0-0026466142 (requires institutional sign-in at Scopus site) 39 CitationsAbstract
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.
Author List
Leone G, Maybaum L, Lee PWAuthor
Gustavo Leone PhD Sr Associate Dean, Director, Professor in the Pathology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Capsid ProteinsProtein Conformation
Protein Structure, Tertiary
Reoviridae
Viral Proteins
