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Membrane topology of the 22 kDa integral peroxisomal membrane protein
Author(s) -
Kaldi K.,
Diestelkötter P.,
Stenbeck G.,
Auerbach S.,
Jäkle U.,
Mägert H.-J.,
Wieland F.T.,
Just W.W.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81167-x
Subject(s) - integral membrane protein , membrane topology , peroxisomal targeting signal , transmembrane protein , peroxisome , membrane protein , complementary dna , cytosol , microbiology and biotechnology , vesicle associated membrane protein 8 , homology (biology) , biochemistry , biology , transmembrane domain , topology (electrical circuits) , membrane , chemistry , gene , enzyme , receptor , mathematics , combinatorics
In order to study the membrane topology and the possible function of the rat liver 22 kDa integral peroxisomal membrane protein (PMP 22) at a molecular level, we have cloned PMP 22 from a λgt11 expression library and sequenced its cDNA. Hydropathy analysis of the deduced primary structure indicates 4 putative transmembrane segments. The accessibility to exogenous aminopeptidase of PMP 22 in intact peroxisomes suggests that the N‐terminus faces the cytosol. A model of the topology of PMP 22 in the peroxisomal membrane is discussed. Homology studies revealed a striking similarity with the Mpv 17 gene product. Lack of this membrane protein causes nephrotic syndrome in mice.

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