Cotranslational folding of proteins

被引:10
作者
Basharov, MA [1 ]
机构
[1] Russian Acad Sci, Inst Theoret & Expt Biophys, Pushchino 142290, Moscow Region, Russia
关键词
protein folding; cotranslational folding; mechanism of folding;
D O I
10.1023/A:1002800822475
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
We suppose that folding of proteins occurs cotranslationally by the following scheme. The polypeptide chains enter the folding sites from protein translocation complexes (ribosome, translocation machinery incorporated in membranes) directionally with the N-terminus and gradually The chain starts to fold as soon as its N-terminal residue enters the folding site from the translocation complex. The folding process accompanies the translocation of the chain to its folding site and is completed after the C-terminal residue leaves the translocation complex. Proteins fold in sequential stages, by translocation of their polypeptide into folding compartments. At each stage a particular conformation of the N-terminal part of the chain that has emerged from the translocation complex is formed. The formation of both the particular conformations of the N-terminal chain segment at each folding stage and the final native protein conformation at the last stage occurs in a time that does not exceed the duration of the fastest elongation cycle on the ribosome.
引用
收藏
页码:1380 / 1384
页数:5
相关论文
共 75 条
[1]   Microsecond protein folding kinetics from native-state hydrogen exchange [J].
Arrington, CB ;
Robertson, AD .
BIOCHEMISTRY, 1997, 36 (29) :8686-8691
[2]   THE CONTROL OF PROTEIN-SYNTHESIS DURING HEAT-SHOCK IN DROSOPHILA CELLS INVOLVES ALTERED POLYPEPTIDE ELONGATION RATES [J].
BALLINGER, DG ;
PARDUE, ML .
CELL, 1983, 33 (01) :103-113
[3]  
Basharov MA, 2000, BIOCHEMISTRY-MOSCOW+, V65, P1184
[4]  
BERGMAN LW, 1979, J BIOL CHEM, V254, P5690
[5]   TRANSFER OF PROTEINS ACROSS MEMBRANES .1. PRESENCE OF PROTEOLYTICALLY PROCESSED AND UNPROCESSED NASCENT IMMUNOGLOBULIN LIGHT-CHAINS ON MEMBRANE-BOUND RIBOSOMES OF MURINE MYELOMA [J].
BLOBEL, G ;
DOBBERSTEIN, B .
JOURNAL OF CELL BIOLOGY, 1975, 67 (03) :835-851
[6]   DOES QUANTITATIVE TRANSFER-RNA ADAPTATION TO CODON CONTENT IN MESSENGER-RNA OPTIMIZE THE RIBOSOMAL TRANSLATION EFFICIENCY - PROPOSAL FOR A TRANSLATION SYSTEM MODEL [J].
CHAVANCY, G ;
GAREL, JP .
BIOCHIMIE, 1981, 63 (03) :187-195
[7]   COTRANSLATIONAL FOLDING AND CALNEXIN BINDING DURING GLYCOPROTEIN-SYNTHESIS [J].
CHEN, W ;
HELENIUS, J ;
BRAAKMAN, I ;
HELENIUS, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (14) :6229-6233
[8]   RIBOSOME-BOUND BETA-GALACTOSIDASE [J].
COWIE, DB ;
DUERKSEN, JD ;
ROBERTS, RB ;
SPIEGELMAN, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1961, 47 (01) :114-&
[9]   PROTEIN-FOLDING - AN UNFOLDING STORY [J].
CREIGHTON, TE .
CURRENT BIOLOGY, 1995, 5 (04) :353-356
[10]   SECRETORY PROTEINS MOVE THROUGH THE ENDOPLASMIC-RETICULUM MEMBRANE VIA AN AQUEOUS, GATED PORE [J].
CROWLEY, KS ;
LIAO, SR ;
WORRELL, VE ;
REINHART, GD ;
JOHNSON, AE .
CELL, 1994, 78 (03) :461-471