D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.
Proc Natl Acad Sci U S A
; 105(30): 10565-70, 2008 Jul 29.
Article
em En
| MEDLINE
| ID: mdl-18647839
ABSTRACT
Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Retroviridae
/
Proteínas Nucleares
/
Membrana Celular
/
Dineínas
/
Proteínas Associadas aos Microtúbulos
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article