Murine MusD retrotransposon: structure and molecular evolution of an "intracellularized" retrovirus.

ABSTRACT: We had previously identified active autonomous copies of the MusD long terminal repeat-retrotransposon family, which have retained transpositional activity. These elements are closely related to betaretroviruses but lack an envelope (env) gene. Here we show that these elements encode strictly intracellular virus-like particles that can unambiguously be identified by electron microscopy. We demonstrate intracellular maturation of the particles, with a significant proportion of densely packed cores for wild-type MusD but not for a protease mutant. We show that the molecular origin of this unexpected intracellular localization is solely dependent on the N-terminal part of the Gag protein, which lacks a functional sequence for myristoylation and plasma membrane targeting: replacement of the N-

SUBMITTER: Ribet D 

PROVIDER: S-EPMC1797557 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature