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PMID:15133130
| Citation |
Rottensteiner, H, Kramer, A, Lorenzen, S, Stein, K, Landgraf, C, Volkmer-Engert, R and Erdmann, R (2004) Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 15:3406-17 |
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| Abstract |
Targeting of peroxisomal membrane proteins (PMPs) is a multistep process that requires not only recognition of PMPs in the cytosol but also their insertion into the peroxisomal membrane. As a consequence, targeting signals of PMPs (mPTS) are rather complex. A candidate protein for the PMP recognition event is Pex19p, which interacts with most PMPs. However, the respective Pex19p-binding sites are ill-defined and it is currently disputed whether these sites are contained within mPTS. By using synthetic peptide scans and yeast two-hybrid analyses, we determined and characterized Pex19p-binding sites in Pex11p and Pex13p, two PMPs from Saccharomyces cerevisiae. The sites turned out to be composed of a short helical motif with a minimal length of 11 amino acids. With the acquired data, it proved possible to predict and experimentally verify Pex19p-binding sites in several other PMPs by applying a pattern search and a prediction matrix. A peroxisomally targeted Pex13p fragment became mislocalized to the endoplasmic reticulum in the absence of its Pex19p-binding site. By adding the heterologous binding site of Pex11p, peroxisomal targeting of the Pex13p fragment was restored. We conclude that Pex19p-binding sites are well-defined entities that represent an essential part of the mPTS. |
| Links |
PubMed PMC452593 Online version:10.1091/mbc.E04-03-0188 |
| Keywords |
Amino Acid Sequence; Binding Sites/genetics; Membrane Proteins/analysis; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Peroxisomes/chemistry; Peroxisomes/metabolism; Protein Sorting Signals; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/analysis; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism; Two-Hybrid System Techniques |
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