Study of WW domain FPB11 agregation
Borges, A.C., Silva, C.L.A., Pires, J.R., Foguel, D. and Silva,J.L
Laboratório de Termodinâmica de Proteínas e Estrutura Viral Gregório Weber., Centro Nacional de Ressonância Magnética nuclear / Instituto de Bioquímica Meica / UFRJ / RJ / Brasil
The WW domain are small proteins that contain tree-stranded and antiparallel b-sheet. They recognize peptides containing proline-rich motifs. The WW domain containing formin binding proteins (FBPs) were originally identified by screening of mouse limb bud expression libraries for binders of a conserved proline-rich region present in formin isoforms.
Formin binding protein 11 (FBP11), localized in the cell nucleus, assumed to be connected to pre-mRNA splicing. We show here that kinetics of light scatering for FBP 11 incubated at 37ºC has three main phases: a lag phase, a burst or growth phase, and finally a plateau. The phase lag was shortened, and the growth phase was acelerated by increasing the protein concetration. WW FBP11 samples were incubated at thioflavin T. A strong increase in emission intensity fluorescence was diagnostic of amyloid formation. We examined the insoluble material by using fluorescence microscopy characterization of FBP11 aggregates. These results suggest that FBP11 aggregates are fiber types.
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