A Scj1p homolog and folding catalysts present in dog pancreas microsomes

被引:39
作者
Bies, C [1 ]
Guth, S [1 ]
Janoschek, K [1 ]
Nastainczyk, W [1 ]
Volkmer, J [1 ]
Zimmermann, R [1 ]
机构
[1] Univ Saarlandes, D-66421 Homburg, Germany
关键词
endoplasmic reticulum; Hsp70; proteins; Hsp40; peptidylprolyl-cis/trans-isomerases; protein disulfide isomerases;
D O I
10.1515/BC.1999.149
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dog pancreas microsomes represent the key components of the established model system for the analysis of protein transport into the mammalian endoplasmic reticulum. More recently, these microsomes were also employed in cell-free systems which address questions related to protein folding and protein degradation in the mammalian endoplasmic reticulum. In order to get at a complete picture of these undoubtedly related processes in the in vitro system we need to know all the proteins we are dealing with, and their respective stoichiometries. Here we give a progress report on our attempts to identify and to quantify the soluble molecular chaperones and folding catalysts which are present in the lumen of dog pancreas microsomes. Eventually, we will need to know how the in vitro system compares with the situation in intact pancreatic cells as well as in other cells.
引用
收藏
页码:1175 / 1182
页数:8
相关论文
共 32 条
[1]  
Baxter BK, 1996, MOL CELL BIOL, V16, P6444
[2]   TRANSFER OF PROTEINS ACROSS MEMBRANES .2. RECONSTITUTION OF FUNCTIONAL ROUGH MICROSOMES FROM HETEROLOGOUS COMPONENTS [J].
BLOBEL, G ;
DOBBERSTEIN, B .
JOURNAL OF CELL BIOLOGY, 1975, 67 (03) :852-862
[3]   ISOLATION OF A MOUSE CDNA-ENCODING MTJ1, A NEW MURINE MEMBER OF THE DNAJ FAMILY OF PROTEINS [J].
BRIGHTMAN, SE ;
BLATCH, GL ;
ZETTER, BR .
GENE, 1995, 153 (02) :249-254
[4]   BIP AND SEC63P ARE REQUIRED FOR BOTH CO- AND POSTTRANSLATIONAL PROTEIN TRANSLOCATION INTO THE YEAST ENDOPLASMIC-RETICULUM [J].
BRODSKY, JL ;
GOECKELER, J ;
SCHEKMAN, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (21) :9643-9646
[5]   Luciferase assembly after transport into mammalian microsomes involves molecular chaperones and peptidyl-prolyl cis/trans-isomerases [J].
Brunke, M ;
Dierks, T ;
Schlotterhose, P ;
Escher, A ;
Schmidt, B ;
Szalay, AA ;
Lechte, M ;
Sandholzer, U ;
Zimmermann, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (38) :23487-23494
[6]   DEFECTIVE CO-TRANSLATIONAL FORMATION OF DISULFIDE BONDS IN PROTEIN DISULFIDE-ISOMERASE-DEFICIENT MICROSOMES [J].
BULLEID, NJ ;
FREEDMAN, RB .
NATURE, 1988, 335 (6191) :649-651
[7]   A novel Hsp7O of the yeast ER lumen is required for the efficient translocation of a number of protein precursors [J].
Craven, RA ;
Egerton, M ;
Stirling, CJ .
EMBO JOURNAL, 1996, 15 (11) :2640-2650
[8]   A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum [J].
Dierks, T ;
Volkmer, J ;
Schlenstedt, G ;
Jung, C ;
Sandholzer, U ;
Zachmann, K ;
Schlotterhose, P ;
Neifer, K ;
Schmidt, B ;
Zimmermann, R .
EMBO JOURNAL, 1996, 15 (24) :6931-6942
[9]   Cer1p, a novel hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast [J].
Hamilton, TG ;
Flynn, GC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (48) :30610-30613
[10]   BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation [J].
Hamman, BD ;
Hendershot, LM ;
Johnson, AE .
CELL, 1998, 92 (06) :747-758