Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Ida J. van der Klei"'
Autor:
Arman Aksit, Ida J. van der Klei
Publikováno v:
International journal of biochemistry & cell biology, 105, 24-34. PERGAMON-ELSEVIER SCIENCE LTD
Peroxisomes are single membrane enclosed cell organelles, which are present in almost all eukaryotic cells. In addition to the common peroxisomal pathways such as beta-oxidation of fatty acids and decomposition of H2O2, these organelles fulfil a rang
Publikováno v:
Biochimica et biophysica acta, 1863(5):17661, 902-910
This contribution describes the phenotypic differences of yeast peroxisome-deficient mutants (pex mutants). In some cases different phenotypes were reported for yeast mutants deleted in the same PEX gene. These differences are most likely related to
Publikováno v:
The Journal of Cell Biology, 211(5), 955-962. ROCKEFELLER UNIV PRESS
The Journal of Cell Biology
The Journal of Cell Biology
Yeast Pex1- and Pex6-deficient cells harbor peroxisomal membrane ghosts that lack matrix proteins but contain all major peroxisomal membrane proteins and acquire matrix proteins to develop into normal peroxisomes upon Pex1 reintroduction.
Pex1 a
Pex1 a
Autor:
Susanne E. Horvath, Ida J. van der Klei, Silke Oeljeklaus, Nils Wiedemann, Ralf M. Zerbes, Inge Perschil, Agnieszka Chacinska, Lena-Sophie Wenz, David A. Stroud, Nikolaus Pfanner, Marten Veenhuis, Günther Daum, Martin van der Laan, Judith M. Müller, Maria Bohnert, Bettina Warscheid, Thomas Becker, Karina von der Malsburg
Publikováno v:
Molecular Biology of the Cell, 23(20), 3948-3956. AMER SOC CELL BIOLOGY
Molecular Biology of the Cell
Molecular Biology of the Cell
The mitochondrial inner membrane organizing system (MINOS) is a large protein complex required for maintaining inner membrane architecture. We report that MINOS independently interacts with both preprotein translocases of the outer mitochondrial memb
Autor:
Thomas Becker, Ida J. van der Klei, Ralf M. Zerbes, Anita M. Kram, Silke Oeljeklaus, Karina von der Malsburg, Martin van der Laan, Nils Wiedemann, Nikolaus Pfanner, Marten Veenhuis, Maria Bohnert, Bettina Warscheid, David A. Stroud
Publikováno v:
Journal of Molecular Biology, 422(2), 183-191. Academic Press
The mitochondrial inner membrane contains a large protein complex crucial for membrane architecture, the mitochondrial inner membrane organizing system (MINOS). MINOS is required for keeping cristae membranes attached to the inner boundary membrane v
Publikováno v:
Autophagy, 7(8), 863-872. Taylor & Francis Group
Evidence is accumulating that damaged components of eukaryotic cells are removed by autophagic degradation (e. g., mitophagy). Here we show that peroxisomes that are damaged by the abrupt removal of the membrane protein Pex3 are massively and rapidly
Autor:
Jan A.K.W. Kiel, Marten Veenhuis, Marleen Otzen, Arjen M Krikken, Shirisha Nagotu, Ida J. van der Klei
Publikováno v:
Traffic, 9(9), 1471-1484. Wiley
We show that Mdv1 and Caf4, two components of the mitochondrial fission machinery in Saccharomyces cerevisiae, also function in peroxisome proliferation. Deletion of MDV1, CAF4 or both, however, had only a minor effect on peroxisome numbers at peroxi
Publikováno v:
FEBS Letters, 581(29), 5627-5634. Wiley
We have analyzed the highly conserved N-terminus of Hansenula polymorpha Pex14p for its function in peroxisomal matrix protein import. The region comprising aa 10-54 of HpPex14p is predicted to contain three alpha-helices. Its alpha-helical structure
Publikováno v:
Fems Yeast Research, 7(7), 1093-1102
We report on the rerouting of peroxisomal alcohol oxidase (AO) to the secretory pathway of Hansenula polymorpha. Using the leader sequence of the Saccharomyces cerevisiae mating factor alpha (MF alpha) as sorting signal, AO was correctly sorted to th
Publikováno v:
Fems Yeast Research, 7(7), 1160-1167
We aim to introduce the penicillin biosynthetic pathway into the methylotrophic yeast Hansenula polymorpha. To allow simultaneous expression of the multiple genes of the penicillin biosynthetic pathway, additional markers were required. To this end,