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Pex11p, a peroxisomal membrane protein required for Pex5p-dependent peroxisome biogenesis, is likely to interact with the peroxisomal membrane in an oligomeric form. To gain an insight into the peroxisomal targeting mechanism of Pex11p, we performed sequence analysis of the C-terminal region of Pex11p and identified sequences rich in lysine (K), arginine (R), and histidine (H) residues. A polypeptide consisting of the KHH sequence bound heme, suggesting that Pex11p contains a heme binding site. In fact, a hemopexin-like sequence (HisHHisR) at the C-terminal region of Pex11p was found to bind heme-derived dimethyl-beta-imidazolylalanine (ImH). When cyanide-bridged Pex11p dimers were reconstituted into liposomes, they showed cooperative binding of ImH and palmitoyl acyl CoAs (PAAc), as well as the heme precursor delta-aminolevulinic acid (ALA) and hematin. The cooperativity of lipid and heme binding was observed with an excess of heme over lipid, and was not seen in the absence of Pex11p. Consequently, these data suggest that the peroxisomal membrane functions as a lipid-lipid and lipid-protein recognition organelle.Cache myelin protein zero is a substrate for nitrated deiminated proteins in experimental autoimmune encephalomyelitis (EAE).
Deimination is an oxidative post-translational modification resulting in the conversion of C-terminal arginine or lysine residues to citrulline. Recently, proteins modified by this novel post-translational process have been implicated in the
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