Membrane topology of the 22 kDa integral peroxisomal membrane protein

K. Kaldi, P. Diestelkötter, G. Stenbeck, S. Auerbach, U. Jäkle, H. J. Mägert, F. T. Wieland, W. W. Just

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)217-222
Number of pages6
JournalFEBS letters
Volume315
Issue number3
DOIs
Publication statusPublished - Jan 11 1993

Keywords

  • Membrane topology
  • Peroxisomal membrane protein, 22 kDa
  • Peroxisome
  • cDNA cloning

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Kaldi, K., Diestelkötter, P., Stenbeck, G., Auerbach, S., Jäkle, U., Mägert, H. J., Wieland, F. T., & Just, W. W. (1993). Membrane topology of the 22 kDa integral peroxisomal membrane protein. FEBS letters, 315(3), 217-222. https://doi.org/10.1016/0014-5793(93)81167-X