Abl structure and conservation, and CTD mutants made in this study.

2017-12-12T18:55:20Z (GMT) by Han S. J. Cheong Mark F. A. VanBerkum
<p>(A) The <i>Drosophila</i> Abl Abl CTD is relatively poorly conserved. (i) Presence of domains annotated by SMART (grey) and motifs (red) in <i>Drosophila</i> Abl. Notable motifs are N-terminal myristoylation site (N-myr), PxxP (P) and EVH1-binding motifs (EVH1). (ii) Conservation of amino acids of Abl in 11 Drosophilid species, as aligned by Clustal Omega and graded using ConSurf. ‘Unreliable’ conservation scores (yellow) have either less than 6 non-gapped residues in the alignment or a confidence interval of equal to or larger than 4 color grades. (iii) Conservation of amino acids using the same methodology as lane 2, but using 40 Abl homologs from both vertebrates and invertebrates. (B) Line cartoon of Drosophila Abl showing the large regions of the CTD (black lines) mutated in this paper. The CTD was divided into halves and quarters. The first quarter was further divided into first and second eighths. All transgenes carry a C-terminal FLAG-tag (not shown). (C) Close-up view of conservation of amino acids in the 1Q region of the Abl CTD, with conservation grade colors as in (A). Also shown are deletions removing the better-conserved second eighth (2E) region, and a comparison to the CR1 deletion as carried out in Rogers et al., 2016 (*). Deletion of the conserved PxxP motif (ΔP) is shown in lane 4. (D) Close-up view of conservation of amino acids in the 3Q region of the Abl CTD Also shown are a deletion removing the EVH1-binding motifs (ΔEVH1), and a deletion removing a highly conserved region of 3Q that includes EVH1 (ΔC).</p>