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- W2090852659 abstract "The HIV accessory protein virion infectivity factor (Vif) is essential for viral replication in CD4+ cells. In the absence of Vif, HIV is efficiently restricted by the cellular cytidine deaminase, APOBEC3G (A3G). Vif recruits a cullin 5 (Cul5)-based ubiquitin ligase and Elongin B/C, which target A3G for proteasomal destruction. Many cullin-based ubiquitin ligases have been shown to oligomerize via their substrate binding motifs. It has also been reported that Vif oligomerizes, but the nature of these oligomers is unknown. We have employed biochemical and biophysical techniques to investigate the oligomeric properties of Vif and Cul5 alone and in complex. Using analytical ultracentrifugation (AUC) we have characterized Vif, Cul5, and Elongin B/C and their complexes. This work will allow for an examination of how the oligomeric state of the free proteins effects the Vif-Cul5 interaction. From these studies we determined that Cul5 dimerizes with a Kd of 70 µM. Our initial studies with Vif (101-153) show little oligomerization. AUC analysis of the Elongin B/C shows that the predominant species is the heterodimer and some higher order oligomerization is observed. We have analyzed the Vif-Cul5-Elongin B/C complex and have seen that the stoichiometry of the complex is 1:1:1:1. Therefore it appears that the oligomeric forms of the individual proteins are not maintained in the complex. It is possible that the sites of self-association occur at the interfaces between the binding partners. To further characterize the Vif-Cul5-Elongin B/C interaction, isothermal titration calorimetry (ITC) was used to define the thermodynamic properties governing association. A thorough understanding of the mechanism of the Vif-Cul5-Elongin B/C complex will shed light on the possible role of oligomerization in both ubiquitin ligase function as well as the function of HIV-1 Vif." @default.
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- W2090852659 date "2011-02-01" @default.
- W2090852659 modified "2023-09-26" @default.
- W2090852659 title "A Hydrodynamic Analysis of the Human Cullin 5 - hIV-1 Vif Ubiquitin Ligase Complex" @default.
- W2090852659 doi "https://doi.org/10.1016/j.bpj.2010.12.2310" @default.
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