Peroxisome targeting signal 1: Is it really a simple tripeptide?

• Published in: Biochimica et biophysica acta Vol. 1763; no. 12; pp. 1565 - 1573
• Main Authors: Brocard, Cécile, Hartig, Andreas
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2006
• Subjects: Amino Acid Motifs; Animals; Humans; Knowledge Bases; Oligopeptides - metabolism; Peroxisome; Peroxisome-Targeting Signal 1 Receptor; Peroxisomes - metabolism; PEX5; Predictor; Protein Sorting Signals; Protein Structure, Tertiary; Protein Transport; PTS1; Receptors, Cytoplasmic and Nuclear - metabolism; Species Specificity; Targeting; Peroxisome; Targeting; Predictor; PTS1; PEX5
• ISSN: 0167-4889; 0006-3002; 1879-2596
• DOI: 10.1016/j.bbamcr.2006.08.022

Originally, the peroxisomal targeting signal 1 (PTS1) was defined as a tripeptide at the C-terminus of proteins prone to be imported into the peroxisomal matrix. The corresponding receptor PEX5 initiates the translocation of proteins by identifying potential substrates via their C-termini and trapping PTS1s through remodeling of its TPR domain. Thorough studies on the interaction between PEX5 and PTS1 as well as sequence-analytic tools revealed the influence of amino acid residues further upstream of the ultimate tripeptide. Altogether, PTS1s should be defined as dodecamer sequences at the C-terminal ends of proteins. These sequences accommodate physical contacts with both the surface and the binding cavity of PEX5 and ensure accessibility of the extreme C-terminus. Knowledge-based approaches in applied Bioinformatics provide reliable tools to accurately predict the peroxisomal location of proteins not yet determined experimentally.