Post-transcriptional Regulatory Functions of Mammalian Pumilio Proteins - PubMed (original) (raw)
(A) Diagrams of human PUM1 and PUM2 proteins showing length in amino acid (aa) residues, sequence motifs, secondary structure, disordered versus ordered regions (computed by JRONN) [119] and hydrophobic versus hydrophilic amino acid content (adapted from Protein Data Bank:
). Post-translational modifications (PTM) including methylation, phosphorylation, and ubiquitylation from Uniprot (
) and Phosphosite (
) are shown at the top. Motifs designated by a single letter represent low complexity regions enriched for that amino acid residue (A = alanine rich, Q = glutamine rich, S = serine rich, G = glycine rich). The TRMs within each Pum repeat (R1-R8) are also shown. (B) Diagram for founding member, Drosophila Pumilio, is shown for comparison. (C) Plot of relative sequence conservation versus amino acid residue position of 82 Pumilio protein orthologs including insects, fish, reptiles, birds, marsupials, mammals, primates and humans, generated using Clustal Omega [120], Consurf server [121], and Emboss Plotcon (
http://www.bioinformatics.nl/cgi-bin/emboss/plotcon
). For reference, conservation is plotted relative to functional domains defined for Drosophila Pumilio including three repression domains (RD1–3), Pumilio Conserved Motifs (PCMa and PCMb), and the Pum repeats (R1-R8) of the Pum- HD. Troughs represent sites of insertion. Peak height is proportional to conservation of sequence identity. (D) Diagrams of the divergent Pumilio orthologs PUM3 and NOP9. Motifs include predicted nuclear localization signals (NLS) and C-terminal Penguin Like (CPL) motif (PFam PF08144).