POSTTRANSLATIONAL PROCESSING OF A CARBOXY-TERMINAL PROPEPTIDE CONTAINING A KDEL SEQUENCE OF PLANT VACUOLAR CYSTEINE ENDOPEPTIDASE (SH-EP)

Authors
OKAMOTO T NAKAYAMA H SETA K ISOBE T MINAMIKAWA T
Citation
T. Okamoto et al., POSTTRANSLATIONAL PROCESSING OF A CARBOXY-TERMINAL PROPEPTIDE CONTAINING A KDEL SEQUENCE OF PLANT VACUOLAR CYSTEINE ENDOPEPTIDASE (SH-EP), FEBS letters, 351(1), 1994, pp. 31-34
Citations number
17
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
351
Issue
1
Year of publication
1994
Pages
31 - 34
Database
ISI
SICI code
0014-5793(1994)351:1<31:PPOACP>2.0.ZU;2-9
Abstract
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 i ntermediate of SH-EP formed in the endoplasmic reticulum is transporte d to protein bodies and processed to the 33 kDa mature form during tra nsport or thereafter, and that the COOH-terminal propeptide of 10 amin o acid residues containing a KDEL sequence, which is known as a retent ion signal for the endoplasmic reticulum lumen, is processed to form t he mature SH-EP.