Results 251 to 260 of about 27,570 (293)

Protein folding in the central cavity of the GroEL–GroES chaperonin complex

Nature, 1996
Jörg Martin, Hediye Erdjument-Bromage, Paul Tempst   +2 more
exaly   +2 more sources

Evidence for GroES Acting as a Transcriptional Regulator

Biochemical and Biophysical Research Communications, 1996
Cochaperonins (cpn10) assist chaperonins (cpn60) in promoting folding and assembly of other proteins. Upon expression of Mycobacterium tuberculosis cpn10 in Escherichia coli we have purified a polypeptide which, through amino acid sequencing, was identified as the endogenous E. coli 10K-S protein.
Legname, Giuseppe, Buono P, Fossati G, Monzini N, Mascagni P, Modena D, Marcucci F.   +6 more
openaire   +2 more sources

GroE Assists Refolding of Recombinant Human Pro-Urokinase

Journal of Biochemistry, 1997
GroE, one of the molecular chaperones, facilitates correct protein folding both in vitro and in vivo. The refolding of recombinant human pro-urokinase, a protein with a high content of disulfide bonds, was used as a model system to illustrate the mechanism of action of GroE.
Z, Xu, S, Yang, D, Zhu
openaire   +2 more sources

Reversible Oligomerization and Denaturation of the Chaperonin GroES

Biochemistry, 1996
The chaperonin GroEL can assist protein folding and normally acts with the co-chaperonin GroES. These Escherichia coli proteins are encoded on the same operon, with GroES positioned first. In this report, we have investigated the reversible folding of GroES. Using fluorescence anisotropy of dansyl-labeled GroES, intrinsic fluorescence, bis-ANS binding,
J W, Seale, B M, Gorovits, J, Ybarra, P M, Horowitz   +3 more
openaire   +2 more sources

Refolding of Barnase in the Presence of GroE

Journal of Molecular Biology, 1993
The refolding of barnase in the presence of GroEL has been monitored on the millisecond to seconds time scale using stopped-flow kinetics. GroEL binds rapidly and tightly to the denatured enzyme with a second-order rate constant of greater than 1.3 x 10(8) s-1 M-1 and slows down greatly the rate of barnase refolding.
T E, Gray, A R, Fersht
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Structure and function of the GroE chaperone

Cellular and Molecular Life Sciences, 2002
The Escherichia coli proteins GroEL and GroES were the first chaperones to be studied in detail and have thus become a role model for assisted protein folding in general. A wealth of both structural and functional data on the GroE system has been accumulated over the past years, enabling us now to understand the basic principles of how this fascinating
openaire   +2 more sources

Phosphofructokinase interacts with molecular chaperonins GroEL and GroES

Acta Biologica Hungarica, 1997
For studying the possible interaction between the chaperonins and phosphofructokinase (PFK), bacterial chaperonins GroEL, GroES, and the PFK were co-purified from chaperonin over-expressing, heat treated E. coli strains. GroEL interacted with PFK in the presence of Mg2+, leading to a gradual decrease in the activity of the enzyme.
B, Melegh, Y, Minami
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GroE-mediated folding of bacterial luciferases in vivo

Molecular and General Genetics MGG, 1993
In this study we present evidence indicating that GroE chaperonins mediate de novo protein folding of heterodimeric and monomeric luciferases under heat shock or sub-heat shock conditions in vivo. The effects of additional groESL and groEL genes on the bioluminescence of Escherichia coli cells expressing different bacterial luciferase genes at various ...
A, Escher, A A, Szalay
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Escherichia coli GroES

1997
Abstract The groE locus maps at 94 minutes on the E. coli chromosome, encodes two polypeptides, GroES, GroEL, in that order (Genbank accession number X07850) (Hemmingsen et al., 1988). The 97 residue GroES polypeptide has a predicted Mr of 10 368 daltons, a pl of 4.92.
A Taher, SJ Landry
openaire   +1 more source

The Escherichia coli groE chaperonins.

Seminars in cell biology, 1991
The E.coli groES and groEL genes have been shown to form an operon, to be essential for E. coli viability, and to belong to the so-called heat-shock class of genes whose expression is regulated by the intracellular levels of sigma factor sigma 32.
C, Georgopoulos, D, Ang
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