Myristate modification does not function as a membrane association signal during poliovirus capsid assembly.
The myristate moiety is required for poliovirus assembly. Unlike most other myristoyl-modified proteins, which are membrane associated, no specific membrane association of the poliovirus capsid proteins or assembly intermediates was observed. Furthermore, no apparent differences in membrane association of wild-type and myristoylation deficient mutant viruses could be detected in this analysis. Thus, during poliovirus assembly, the myristate modification is not required as a membrane targeting signal but is more likely involved in structural interactions between protomer subunits.
Lee
Y M
YM
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Chow
M
M
D002213:Capsid / Q000378:metabolism*; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D066298:In Vitro Techniques; D009024:Morphogenesis; D009226:Myristates / Q000378:metabolism*; D017955:Poliovirus / Q000254:growth & development*; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D014779:Virus Replication
D009226:Myristates; D011498:Protein Precursors