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Not all primate RanBP2 proteins are the same.

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posted on 2018-03-08, 18:49 authored by Nicholas R. Meyerson, Cody J. Warren, Daniel A. S. A. Vieira, Felipe Diaz-Griferro, Sara L. Sawyer

A) A domain diagram of RanBP2 is shown. TPR, tetratricopeptide; RBD, Ran binding domain; Cyp, Cyclophilin. B) Protein schematic of TRIM-fusion constructs showing the tripartite RING/B-Box/Coiled-coil (RBCC) domain fused to a cyclophilin domain. C) CRFK cell lines transduced to stably express different TRIM-RanCyps (bottom) were infected with VSV-G pseudotyped HIV-1, FIV, or NB-MLV, all encoding a GFP reporter. The percentage of cells infected in each sample was normalized to the empty vector control. A western blot detecting HA-tagged TRIM-RanCyp constructs is shown along with a β-actin loading control. Infections were performed in triplicate and error bars represent twice the standard error of the mean. D) Partial protein alignment of the RanCyp domain from primates in C. Here, residue coordinates refer to the coordinates of the human RanCyp domain (see exact numbering scheme in S1 Fig; 3060 needs to be added to these numbers to convert them to the residue position in full-length human RanBP2). Asterisks (*) indicate conserved residues. Red text indicates species-specific differences at non-conserved sites.

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