A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses

Citation
M. Shmulevitz et R. Duncan, A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses, EMBO J, 19(5), 2000, pp. 902-912
Citations number
70
Categorie Soggetti
Molecular Biology & Genetics
Journal title
EMBO JOURNAL
ISSN journal
02614189 → ACNP
Volume
19
Issue
5
Year of publication
2000
Pages
902 - 912
Database
ISI
SICI code
0261-4189(20000301)19:5<902:ANCOFS>2.0.ZU;2-X
Abstract
The non-enveloped fusogenic avian and Nelson Bay reoviruses encode homologo us 10 kDa non-structural transmembrane proteins. The p10 proteins Localize to the cell surface of transfected cells in a type I orientation and induce efficient cell-cell fusion, Mutagenic studies revealed the importance of c onserved sequence-predicted structural motifs in the membrane association a nd fusogenic properties of p10. These moths included a centrally located tr ansmembrane domain, a conserved cytoplasmic basic region, a small hydrophob ic moth in the N-terminal domain and four conserved cysteine residues. Func tional analysis indicated that the extreme C-terminus of p10 functions in a sequence-independent manner to effect p10 membrane localization, while the N-terminal domain displays a sequence-dependent effect on the fusogenic pr operty of p10. The small size, unusual arrangement of structural motifs and lack of any homologues in previously described membrane fusion proteins su ggest that the fusion-associated small transmembrane (FAST) proteins of reo virus represent a new class of membrane fusion proteins.