Binding of coatomer by the PEX11 C‐terminus is not required for function

FEBS Letters

Schulreich, Sebastian²  Bremser, Martina¹  Maier, Alexander G.²  Clayton, Christine² 

[1] Biochemiezentrum (BZH), University of Heidelberg, Heidelberg, Germany;Zentrum für Molekulare Biologie (ZMBH), University of Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

关键词: Trypanosome;    Microbody;    Glycosome;    Coatomer;    PEX11;    COP;    coat proteins;    GAPDH;    glyceraldehyde 3-phosphate dehydrogenase;    tet;    tetracycline;    ARF;    ADP-ribosylation factor;    DTT;    dithiothreitol;    TCA;    trichloroacetic acid;    PEX11 proteins are PEX11 in trypanosomes;    Pex11p in Saccharomyces cerevisiae and Pex11 in mammals;   

DOI  :  10.1016/S0014-5793(00)02132-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Microbodies are single membrane-bound organelles found in eukaryotes from trypanosomes to man. Although they have diverse roles in metabolism, the mechanisms and molecules involved in membrane biogenesis and matrix protein import are conserved. Similarly, the basic mechanisms and structures involved in vesicular transport are similar throughout eukaryotic evolution. The PEX11 proteins are required for the division of microbodies in trypanosomes, yeast and mammals, and a role of coatomer in this process has been suggested. We show here that the binding of trypanosome, yeast and bovine coatomers to selected peptides is identical. Coatomer binds to the C-termini of trypanosome PEX11 and rat Pex11α, but not yeast Pex11p or human Pex11β. Mutations of the C-terminus of trypanosome PEX11 that eliminated coatomer binding did not affect function in yeast or trypanosomes. Thus binding of coatomer to the C-terminus of PEX11 is not required for PEX11 function.

【 授权许可】

Unknown