\'C-terminal truncation\' reduces oligomerization
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Recombinant z protein forms active oligomers with apparent molecular weight ranging from dimers to 5 MDa. C-terminal deletion reduces the apparent molecular weight of oligomers to a maximum of 440 kDa.
Recombinant protein was centrifuged for 10 minutes and the distribution of z protein in the pellet and the supernatant was monitored by western blot.
Interaction in vitro; protein produced by in vitro translation.
Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.
Recombinant z protein forms 14.2S particles.
L518P or L518D
Y510Δ
L550Q
L555Q
Interaction in vitro; protein produced and labeled by in vitro translation.
Most z oligomers elute in the exclusion volume of the gel filtration column (> 2000 kDa).
Interaction in vitro; protein produced and labeled by in vitro translation.
Source was nuclear extract of Sf9 cell line; protein produced from transfected constructs.
Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).
Two-hybrid system: yeast GAL4-BD/GAL4-AD
Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).
