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pro vyhledávání: '"Ralf van Dijk"'
Autor:
Paulina Ozimek, Marten Veenhuis, Kantcho Latchev, Ida J. van der Klei, Carlos Gancedo, Ralf van Dijk, Dong Yuan Wang
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Molecular Biology of the Cell, 14(2), 786-797. AMER SOC CELL BIOLOGY
instname
Molecular Biology of the Cell, 14(2), 786-797. AMER SOC CELL BIOLOGY
12 páginas, 10 figuras.-- et al.
Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, whereas other peroxisomal matrix proteins are normally activated and sorted to pe
Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, whereas other peroxisomal matrix proteins are normally activated and sorted to pe
Autor:
Anne Koek, Marten Veenhuis, Klaas Nico Faber, Ineke Keizer-Gunnink, Ralf van Dijk, Ida J. van der Klei
Publikováno v:
Biochimica et Biophysica Acta-Molecular Cell Research, 1591(1-3):PII S0167-4889(02)00274-4, 157-162. ELSEVIER SCIENCE BV
Previously, Waterham et al. [EMBO J. 12 (1993) 4785] reported that cytosolic oligomeric alcohol oxidase (AO) is not incorporated into peroxisomes after reassembly of the organelles in the temperature-sensitive peroxisome-deficient mutant pex1-6(ts) o
Publikováno v:
Molecular Biology of the Cell, 15(3), 1347-1355. AMER SOC CELL BIOLOGY
Import of Hansenula polymorpha alcohol oxidase (AO) into peroxisomes is dependent on the PTS1 receptor, HpPex5p. The PTS1 of AO (-LARF) is sufficient to direct reporter proteins to peroxisomes. To study AO sorting in more detail, strains producing mu
Publikováno v:
Fems Yeast Research, 2(1):PII S1567-1356(01)00057-5, 17-24
The Hansenula polymorpha genes encoding the putative functional homologs of the enzymes involved in the seventh and eighth step in purine biosynthesis, HpPUR7 and HpPUR8, were cloned and sequenced. An overexpression vector designated pHIPA4 was const
Publikováno v:
Fems Yeast Research, 1(4)
Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1938726a8fdeeaf9d2fe38d7106ea17
https://doi.org/10.1111/j.1567-1364.2002.tb00043.x
https://doi.org/10.1111/j.1567-1364.2002.tb00043.x
Publikováno v:
Molecular Biology of the Cell; March 2004, Vol. 15 Issue: 3 p1347-55, 9p
Publikováno v:
Biochimica et Biophysica Acta-Molecular Cell Research, 1542(1-3):PII S0167-4889(01)00176-8, 160-172. ELSEVIER SCIENCE BV
A protease activity has been partially purified from peroxisomal matrix fractions of the methylotrophic yeast Candida hoidinii. The enzyme migrates as a single peak on a sucrose velocity gradient with an apparent native molecular mass of similar to 8