Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15).
作者： Markus BUCHLER , Ursula TISLJAR , Dieter H. WOLF
DOI: 10.1111/J.1432-1033.1994.TB19978.X
关键词: Protein degradation 、 Thimet oligopeptidase 、 Metalloendopeptidase 、 Nucleic acid sequence 、 Saccharolysin 、 Biochemistry 、 Biology 、 Open reading frame 、 Oligopeptidase 、 Mutant 、 Molecular biology
摘要: The yeast PRD1 gene, encoding proteinase yscD, was cloned by complementation of the prd1-6 point mutation. Sequencing gene revealed an open reading frame 2.136 kb, a protein 712 amino acids with calculated molecular mass 81.8 kDa. sequence HEGLG beginning at residue 501 represents HEXXH motif, unique for zinc metallo-peptidases. Sequence comparison complete identity yscD recently published chromosome III. We found 34.8% between and rat metalloendopeptidase (thimet oligopeptidase, EP 24.15). Proteinase hydrolyzes several chromogenic fluorogenic peptides that are substrates thimet oligopeptidase. N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-p-aminobenzoic acid, compound designed as specific inhibitor 24.15, is also strong enzyme. non-vacuolar 3–5% total enzyme activity can be detected in intermembrane space mitochondria. In mutant carrying deletion no detectable cytoplasm mitochondria these cells. They do not show any grossly altered phenotype but exhibit decrease intracellular degradation peptides. This suggests function late stages degradation.
sci-hub.se 参考文章(83)
W. Heinemeyer, J. A. Kleinschmidt, J. Saidowsky, C. Escher, D. H. Wolf, Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. The EMBO Journal. ,vol. 10, pp. 555- 562 ,(1991) , 10.1002/J.1460-2075.1991.TB07982.X
Harvey Miller, [13] Practical aspects of preparing phage and plasmid DNA: Growth, maintenance, and storage of bacteria and bacteriophage Methods in Enzymology. ,vol. 152, pp. 145- 170 ,(1987) , 10.1016/0076-6879(87)52016-X
B S Hartley, Strategy and tactics in protein chemistry Biochemical Journal. ,vol. 119, pp. 805- 822 ,(1970) , 10.1042/BJ1190805F
Robert L. Hill, Ralph A. Bradshaw, [17] Fumarase Citric Acid Cycle. ,vol. 13, pp. 91- 99 ,(1969) , 10.1016/0076-6879(69)13021-9
J L Bennetzen, B D Hall, The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. Journal of Biological Chemistry. ,vol. 257, pp. 3018- 3025 ,(1982) , 10.1016/S0021-9258(19)81067-0
T Achstetter, C Ehmann, A Osaki, D H Wolf, Proteolysis in eukaryotic cells. Proteinase yscE, a new yeast peptidase. Journal of Biological Chemistry. ,vol. 259, pp. 13344- 13348 ,(1984) , 10.1016/S0021-9258(18)90700-3
G Daum, P C Böhni, G Schatz, Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. Journal of Biological Chemistry. ,vol. 257, pp. 13028- 13033 ,(1982) , 10.1016/S0021-9258(18)33617-2
Nieves GARCIA-ALVAREZ, Ulrich TEICHERT, Dieter H. WOLF, Proteinase yscD mutants of yeast. Isolation and characterization. FEBS Journal. ,vol. 163, pp. 339- 346 ,(1987) , 10.1111/J.1432-1033.1987.TB10805.X
Steve G Oliver, Quirina JM van der Aart, Maria L Agostoni-Carbone, Michel Aigle, Lilia Alberghina, Despina Alexandraki, G Antoine, R Anwar, JPG Ballesta, P Benit, G Berben, Elisabetta Bergantino, N Biteau, PA Bolle, M Bolotin-Fukuhara, A Brown, AJP Brown, JM Buhler, C Carcano, G Carignani, H Cederberg, R Chanet, R Contreras, M Crouzet, B Daignan-Fornier, E Defoor, M Delgado, J Demolder, C Doira, E Dubois, B Dujon, A Dusterhoft, D Erdmann, M Esteban, F Fabre, C Fairhead, G Faye, H Feldmann, W Fiers, MC Francingues-Gaillard, L Franco, L Frontali, H Fukuhara, LJ Fuller, P Galland, ME Gent, D Gigot, V Gilliquet, N Glansdorff, A Goffeau, M Grenson, P Grisanti, LA Grivell, M De Haan, M Haasemann, D Hatat, J Hoenicka, J Hegemann, CJ Herbert, F Hilger, S Hohmann, CP Hollenberg, K Huse, F Iborra, KJ Indje, K Isono, C Jacq, M Jacquet, CM James, JC Jauniaux, Y Jia, A Jimenez, A Kelly, U Kleinhans, P Kreisl, Gerolamo Lanfranchi, C Lewis, CG Vanderlinden, G Lucchini, K Lutzenkirchen, MJ Maat, L Mallet, G Mannhaupet, E Martegani, A Mathieu, CTC Maurer, D McConnell, RA McKee, F Messenguy, HW Mewes, F Molemans, MA Montague, M Muzi Falconi, L Navas, CS Newlon, D Noone, C Pallier, L Panzeri, BM Pearson, J Perea, P Philippsen, A Pierard, RJ Planta, P Plevani, B Poetsch, F Pohl, B Purnelle, M Ramezani Rad, SW Rasmussen, A Raynal, M Remacha, P Richterich, AB Roberts, F Rodriguez, E Sanz, I Schaaff-Gerstenschlager, B Scherens, B Schweitzer, Y Shu, J Skala, PP Slonimski, F Sor, C Soustelle, R Spiegelberg, LI Stateva, HY Steensma, S Steiner, A Thierry, G Thireos, M Tzermia, LA Urrestarazu, Giorgio Valle, I Vetter, JC van Vliet-Reedijk, M Voet, G Volckaert, P Vreken, H Wang, JR Warmington, D Von Wettstein, BL Wicksteed, C Wilson, H Wurst, G Xu, A Yoshikawa, FK Zimmermann, JG Sgouros, None, The complete DNA sequence of yeast chromosome III. Nature. ,vol. 357, pp. 38- 46 ,(1992) , 10.1038/357038A0
Fred Sherman, Gerald R. Fink, James B. Hicks, Methods in yeast genetics Cold Spring Harbor Laboratory. ,(1979)