Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis

被引:19
作者
Danziger, Oded [1 ]
Shimon, Liat [1 ]
Horovitz, Amnon [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel
关键词
chaperonins; molecular chaperones; allostery; cooperativity; protein folding;
D O I
10.1110/ps.062100606
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
The ATPase activity of many types of molecular chaperones is stimulated by polypeptide substrate binding via molecular mechanisms that are, for the most part, unknown. Here, we report that such stimulation of the ATPase activity of GroEL is abolished when its conserved apical domain residue Glu257 is replaced by alanine. This mutation is also found to convert the ATPase profile of GroEL, a group I chaperonin, into one that is characteristic of group II chaperonins. Steady-state and transient kinetic analysis indicate that both effects are due, at least in part, to a reduction of the affinity of GroEL for ADP. This finding indicates that nonfolded proteins stimulate ATP hydrolysis by accelerating the off-rate of the ADP formed, thereby allowing more rapid cycles of ATP binding and hydrolysis.
引用
收藏
页码:1270 / 1276
页数:7
相关论文
共 33 条
[1]   Inter-ring communication is disrupted in the GroEL mutant Arg13->Gly; Ala126->Val with known crystal structure [J].
Aharoni, A ;
Horovitz, A .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 258 (05) :732-735
[2]   Crystal structure of wild-type chaperonin GroEL [J].
Bartolucci, C ;
Lamba, D ;
Grazulis, S ;
Manakova, E ;
Heumann, H .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 354 (04) :940-951
[3]   THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].
BRAIG, K ;
OTWINOWSKI, Z ;
HEGDE, R ;
BOISVERT, DC ;
JOACHIMIAK, A ;
HORWICH, AL ;
SIGLER, PB .
NATURE, 1994, 371 (6498) :578-586
[4]  
Brocchieri L, 2000, PROTEIN SCI, V9, P476
[5]   Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli [J].
Brune, M ;
Hunter, JL ;
Howell, SA ;
Martin, SR ;
Hazlett, TL ;
Corrie, JET ;
Webb, MR .
BIOCHEMISTRY, 1998, 37 (29) :10370-10380
[6]   DIRECT, REAL-TIME MEASUREMENT OF RAPID INORGANIC-PHOSPHATE RELEASE USING A NOVEL FLUORESCENT-PROBE AND ITS APPLICATION TO ACTOMYOSIN SUBFRAGMENT-1 ATPASE [J].
BRUNE, M ;
HUNTER, JL ;
CORRIE, JET ;
WEBB, MR .
BIOCHEMISTRY, 1994, 33 (27) :8262-8271
[7]   A structural model for GroEL-polypeptide recognition [J].
Buckle, AM ;
Zahn, R ;
Fersht, AR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) :3571-3575
[8]   THE ORIGINS AND CONSEQUENCES OF ASYMMETRY IN THE CHAPERONIN REACTION CYCLE [J].
BURSTON, SG ;
RANSON, NA ;
CLARKE, AR .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 249 (01) :138-152
[9]   The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity [J].
Chen, LL ;
Sigler, PB .
CELL, 1999, 99 (07) :757-768
[10]   RESIDUES IN CHAPERONIN GROEL REQUIRED FOR POLYPEPTIDE BINDING AND RELEASE [J].
FENTON, WA ;
KASHI, Y ;
FURTAK, K ;
HORWICH, AL .
NATURE, 1994, 371 (6498) :614-619