title: Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p.
abstract: Kinetoplastid protozoa confine large parts of glycolysis within glycosomes, which are microbodies related to peroxisomes. We cloned the gene encoding the second most abundant integral membrane protein of Trypanosoma brucei glycosomes. The 24 kDa protein is very basic and hydrophobic, with two predicted transmembrane domains. It is targeted to peroxisomes when expressed in mammalian cells and yeast. The protein is a functional homologue of Pex11p from Saccharomyces cerevisiae: pex11Delta mutants, which are defective in peroxisome proliferation, can be complemented by the trypanosome gene. Sequence conservation is significant in the N- and C-terminal domains of all putative Pex11p homologues known, from trypanosomes, yeasts and mammals. Several lines of evidence indicate that these domains are oriented towards the cytosol. TbPex11p can form homodimers, like its yeast counterpart. The TbPEX11 gene is essential in trypanosomes. Inducible overexpression of the protein in T.brucei bloodstream forms causes growth arrest, the globular glycosomes being transformed to clusters of long tubules filling significant proportions of the cytoplasm. Reduced expression results in trypanosomes with fewer, but larger, organelles.
authors.affiliation: Zentrum für Molekulare Biologie, Universität Heidelberg, Im Neuenheimer Feld 282.
authors.forename: P
authors.initials: P
authors.lastname: Lorenz
authors.forename: A G
authors.initials: AG
authors.lastname: Maier
authors.forename: E
authors.initials: E
authors.lastname: Baumgart
authors.forename: R
authors.initials: R
authors.lastname: Erdmann
authors.forename: C
authors.initials: C
authors.lastname: Clayton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002455:Cell Division; D002460:Cell Line; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D003600:Cytosol; D016054:DNA, Protozoan; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics; D015870:Gene Expression; D017125:Genes, Protozoan; D008562:Membrane Glycoproteins / Q000235:genetics*; D008565:Membrane Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008830:Microbodies / Q000378:metabolism; D008969:Molecular Sequence Data; D015388:Organelles / Q000502:physiology; D000074401:Peroxins; D015800:Protozoan Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000502:physiology*; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D014346:Trypanosoma brucei brucei / Q000235:genetics / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*
chemical_list: D016054:DNA, Protozoan; D005656:Fungal Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C092128:PEX11 protein, S cerevisiae; D000074401:Peroxins; C490454:Pex11a protein, rat; D015800:Protozoan Proteins; D029701:Saccharomyces cerevisiae Proteins; C113754:p24 protein, Trypanosoma