title: D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.
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.
authors.affiliation: Laboratory of NMR Spectroscopy and Department of Biochemistry and Microbiology and Center of Applied Genomics, Institute of Chemical Technology, Prague, Technická 5, 16628 Prague, Czech Republic.
authors.forename: Jirí
authors.initials: J
authors.lastname: Vlach
authors.forename: Jan
authors.initials: J
authors.lastname: Lipov
authors.forename: Michaela
authors.initials: M
authors.lastname: Rumlová
authors.forename: Václav
authors.initials: V
authors.lastname: Veverka
authors.forename: Jan
authors.initials: J
authors.lastname: Lang
authors.forename: Pavel
authors.initials: P
authors.lastname: Srb
authors.forename: Zdenek
authors.initials: Z
authors.lastname: Knejzlík
authors.forename: Iva
authors.initials: I
authors.lastname: Pichová
authors.forename: Eric
authors.initials: E
authors.lastname: Hunter
authors.forename: Richard
authors.initials: R
authors.lastname: Hrabal
authors.forename: Tomás
authors.initials: T
authors.lastname: Ruml
mesh_terms: D000818:Animals; D001665:Binding Sites; D001692:Biological Transport; D019556:COS Cells; D002462:Cell Membrane / Q000378:metabolism* / Q000821:virology*; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000378:metabolism; D004398:Dyneins / Q000378:metabolism*; D006801:Humans; D016093:Mason-Pfizer monkey virus / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D009154:Mutation; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D010641:Phenotype; D017434:Protein Structure, Tertiary; D012190:Retroviridae / Q000378:metabolism*; D056427:t-Complex Genome Region
chemical_list: D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D004398:Dyneins