Proteinase yscE of yeast shows homology with the 20 S cylinder particles of Xenopus laevis

FEBS Letters

Wolf, Dieter H.¹  Escher, Claudia¹  Kleinschmidt, Jürgen A.² 

[1] Biochemisches Institut der Universität Freiburg, Hermann-Herder-Str. 7, D-7800 Freiburg, FRG;Deutsches Krebsforschungszentrum, Institut für Zell- und Tumorbiologie, Im Neuenheimer Feld 280, D-6900 Heidelberg, FRG

关键词: Proteinase yscE;    20 S particle;    Nucleus;    (Saccharomyces cerevisiae;    Xenopus laevis);   

DOI  :  10.1016/0014-5793(88)80540-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proteinase yscE of the yeast Saccharomyces cerevisiae has been compared with the 20 S cylinder particles of Xenopus laevis. Both proteins are characterized by a similar group of 10–12 polypeptides with molecular masses ranging between 21 and 38 kDa. Antibodies generated against the 20 S Xenopus cylinder particles show cross-reactivity with yeast proteinase yscE subunits. The Xenopus particles and yeast proteinase yscE exhibit an identical image in electron microscopy. Both proteins appear as hollow cylinders mostly composed of four stacked annuli. The Xenopus 20 S particles exhibit proteolytic activity against the three peptide derivatives known to be substrates of proteinase yscE. The pH optimum for activity and the inhibition spectrum of the proteolytic activities of Xenopus 20 S particles and of yeast proteinase yscE are identical. The RNA content of the cylinder particles and of proteinase yscE is below 0.1 RNA chain per molecule. Our data suggest that proteinase yscE from yeast and the 20 S cylinder particles of X. laevis are homologous, highly conserved proteins carrying the catalytic character of a peptidase.

【 授权许可】

Unknown