Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones

FEBS Letters

Koga, Mihoko³  Takagi, Hiroshi³  Yabuta, Yukihiro³  Inouye, Masayori¹  Nakamori, Shigeru³  Katsurada, Saori³  Shinde, Ujwal² 

[1] Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA;Department of Biochemistry and Molecular Biology, MRB631, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Mail code: L224, Portland, OR 97201-3098, USA;Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjojima, Matsuoka-cho, Fukui 910-1195, Japan

关键词: Propeptide;    Intramolecular chaperone;    Protein folding;    Subtilisin E;    Aqualysin I;    Chimeric protease;    IMC;    intramolecular chaperone;    SBE;    subtilisin E;    AQI;    aqualysin I;    ProS;    propeptide of subtilisin E;    ProA;    propeptide of aqualysin I;    PAGE;    polyacrylamide gel electrophoresis;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(01)03053-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Several proteases require propeptides for the correct folding of their own protease domain. We have recently found that the propeptide from a thermostable subtilisin homolog aqualysin I can refold subtilisin BPN′ when added in trans. Here, we constructed chimeric genes with subtilisin E and aqualysin I to attempt the in cis folding of subtilisin E by means of the propeptide of aqualysin I. Our results indicate that the propeptide of aqualysin I can to some extent chaperone the intramolecular folding of the denatured subtilisin E. These results suggest that propeptides in the subtilisin family, despite their sequence diversity, have similar functions. Further, some enzymatic properties of some chimeras in which the subtilisin mature domain is partly swapped with that of aqualysin I were shown to be more similar to those of aqualysin I.

【 授权许可】

Unknown