Identification of novel F-box proteins in Xenopus laevis Julie D Regan-Reimann, Quoc Vong Duong, Peter K Jackson  Current Biology  Volume 9, Issue 20, Pages R762-R763 (October 1999) DOI: 10.1016/S0960-9822(00)80006-8 Copyright © 1999 Elsevier Science Ltd Terms and Conditions

Figure 1 A family of F-box proteins in Xenopus laevis, isolated through their ability to bind Skp1. (a) Alignment of F-box domain sequences. The F-box domains from Fbl5, Fbl13, Fbx26, Fbx27 and Fbx28 were aligned using CLUSTAL V. The consensus sequence is shown above. Red, most highly conserved; blue, highly conserved; underline, similar. Dots indicate gaps. The clones were isolated the following number of times: Fbl5 (3), Fbl13 (1), Fbx26 (395), Fbx27 (5), Fbx28 (1). (b) Schematic representation of the domain structures of X. laevis F-box proteins. Current Biology 1999 9, R762-R763DOI: (10.1016/S0960-9822(00)80006-8) Copyright © 1999 Elsevier Science Ltd Terms and Conditions

Figure 2 Phylogenetic tree showing evolutionary relationships within the subfamily of F-box proteins characterized by leucine-rich repeats. Ce, Caenorhabditis elegans; Hs, Homo sapiens; Mm, Mus musculus; Sc, Saccharomyces cerevisiae; Sp, Schizosaccharomyces pombe; Xl, X. laevis. Current Biology 1999 9, R762-R763DOI: (10.1016/S0960-9822(00)80006-8) Copyright © 1999 Elsevier Science Ltd Terms and Conditions