Posttranslational processing of a carboxy‐terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH‐EP)

FEBS Letters

Seta, Kazuo¹  Nakayama, Hiroshi¹  Minamikawa, Takao²  Isobe, Toshiaki¹  Okamoto, Takashi² 

[1] Department of Chemistry, Tokyo Metropolitan University, 1-1 Minami-osawa, Hachioji, Tokyo 192-03, Japan;Department of Biology, Tokyo Metropolitan University, 1-1 Minami-osawa, Hachioji, Tokyo 192-03, Japan

关键词: Cysteine endopeptidase;    Posttranslational processing;    Protein body;    KDEL sequence;    COOH-terminal propeptide;    CNBr;    cyanogen bromide;    EDTA;    ethylenediaminetetraacetic acid;    ER;    endoplasmic reticulum;    HPLC;    high-pressure liquid chromatography;    ME;    2-mercaptoethanol;    MES;    2-morpholino-ethanesulfonic acid;    SDS;    sodium dodecylsulfate;   

DOI  :  10.1016/0014-5793(94)00809-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A plant cysteine endopeptidase, designated SH-EP, is a major protease occurring in cotyledons of Vigna mungo seedlings, and acts to degrade seed globulin stored in protein bodies. Here we show that the 43 kDa intermediate of SH-EP formed in the endoplasmic reticulum is transported to protein bodies and processed to the 33 kDa mature form during transport or thereafter, and that the COOH-terminal propeptide of 10 amino acid residues containing a KDEL sequence, which is known as a retention signal for the endoplasmic reticulum lumen, is processed to form the mature SH-EP.

【 授权许可】

Unknown