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.

• MeSH
• biologické modely MeSH
• biologický transport MeSH
• buněčná membrána metabolismus   virologie   MeSH
• Cercopithecus aethiops MeSH
• COS buňky MeSH
• cytoplazma metabolismus   MeSH
• dyneiny metabolismus   MeSH
• fenotyp MeSH
• genomová oblast t-komplexu MeSH
• jaderné proteiny chemie   metabolismus   fyziologie   MeSH
• lidé MeSH
• Masonův-Pfizerův opičí virus metabolismus   MeSH
• mutace MeSH
• proteiny asociované s mikrotubuly chemie   metabolismus   fyziologie   MeSH
• Retroviridae metabolismus   MeSH
• terciární struktura proteinů MeSH
• vazebná místa MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• dyneiny MeSH
• jaderné proteiny MeSH
• proteiny asociované s mikrotubuly MeSH