Myristoylation drives dimerization of matrix protein from mouse mammary tumor virus.

ABSTRACT:

Background

Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the plasma membrane (PM) and is required for the assembly of most retroviruses. In betaretroviruses, which assemble immature particles in the cytoplasm, myristoylation is dispensable for assembly but is crucial for particle transport to the PM. Oligomerization of HIV-1 MA stimulates the transition of the myristoyl group from a sequestered to an exposed conformation, which is more accessible for membrane binding. However, for other retroviruses, the effect of MA oligomerization on myristoyl group exposure has not been thoroughly investigated.

Results

Here, we demonstrate that MA from the betaretrovirus mouse mammary tumor virus (MMTV) forms dimers in solution and that

SUBMITTER: Dolezal M 

PROVIDER: S-EPMC4700671 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature