caa a22 4500 469093390 CHVBK 20180323133024.0 cr unu---uuuuu 170328e19920801xx s 000 0 eng 10.1007/BF00584463 doi (NATIONALLICENCE)springer-10.1007/BF00584463 Peroxisome biogenesis in Saccharomyces cerevisiae [Elektronische Daten] [Wolf-H. Kunau, Andreas Hartig] The observation that peroxisomes ofSaccharomyces cerevisiae can be induced by oleic acid has opened the possibility to investigate the biogenesis of these organelles in a biochemically and genetically well characterized organism. Only few enzymes have been identified as peroxisomal proteins inSaccharomyces cerevisiae so far; the three enzymes involved in β-oxidation of fatty acids, enzymes of the glyoxylate cycle, catalase A and the PAS3 gene product have been unequivocally assigned to the peroxisomal compartment. However, more proteins are expected to be constituents of the peroxisomes inSaccharomyces cerevisiae. Mutagenesis ofSaccharomyces cerevisiae cells gave rise to mutants unable to use oleic acid as sole carbon source. These mutants could be divided in two groups: those with defects in structural genes of β-oxidation enzymes (fox-mutants) and those with defects in peroxisomal assembly (pas-mutants). All fox-mutants possess morphologically normal peroxisomes and can be assigned to one of three complementation groups (FOX1, 2, 3). All three FOX genes have been cloned and characterized. The pas-mutants isolated are distributed among 13 complementation groups and represent 3 different classes: peroxisomes are either morphologically not detectable (type I) or present but non-proliferating (type II). Mislocalization concerns all peroxisomal proteins in cells of these two classes. The third class of mutants contains peroxisomes normal in size and number, however, distinct peroxisomal matrix proteins are mislocalized (type III). Five additional complementation groups were found in the laboratory of H.F. Tabak. Not all PAS genes have been cloned and characterized so far, and only for few of them the function could be deduced from sequence comparisons. Proliferation of microbodies is repressed by glucose, derepressed by non-fermentable carbon sources and fully induced by oleic acid. The regulation of four genes encoding peroxisomal proteins (PAS1, CTA1, FOX2, FOX3) occurs on the transcriptional level and reflects the morphological observations: repression by glucose and induction by oleic acid. Moreover, trans-acting factors like ADR1, SNF1 and SNF4, all involved in derepression of various cellular processes, have been demonstrated to affect transcriptional regulation of genes encoding peroxisomal proteins. The peroxisomal import machinery seems to be conserved between different organisms as indicated by import of heterologous proteins into microbodies of different host cells. In addition, many peroxisomal proteins contain C-terminal targeting signals. However, more than one import route into peroxisomes does exist. Dissection of the import mechanism in a genetically well suited organism likeSaccharomyces cerevisiae together with further characterization and functional assignment of the PAS gene products will provide insight into the biogenesis of peroxisomes. Moreover, these studies will lead to a good model system for elucidation of the mechanisms underlying human peroxisomal disorders. Kluwer Academic Publishers, 1992 biogenesis nationallicence gene expression nationallicence mutants nationallicence peroxisomes nationallicence yeast nationallicence Kunau Wolf-H Abteilung Zellbiochemie, Institut für Physiologische Chemie, Medizinische Fakultät der Ruhr-Universität, D-4630, Bochum, Germany aut Hartig Andreas Institut für Allgemeine Biochemie der Universität, Währinger Strasse 38, A-1090, Wien, Austria aut Antonie van Leeuwenhoek Kluwer Academic Publishers 62/1-2(1992-08-01), 63-78 0003-6072 62:1-2<63 1992 62 10482 https://doi.org/10.1007/BF00584463 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00584463 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kunau Wolf-H Abteilung Zellbiochemie, Institut für Physiologische Chemie, Medizinische Fakultät der Ruhr-Universität, D-4630, Bochum, Germany aut NATIONALLICENCE 700 1- Hartig Andreas Institut für Allgemeine Biochemie der Universität, Währinger Strasse 38, A-1090, Wien, Austria aut NATIONALLICENCE 773 0- Antonie van Leeuwenhoek Kluwer Academic Publishers 62/1-2(1992-08-01), 63-78 0003-6072 62:1-2<63 1992 62 10482 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer