Results 191 to 200 of about 23,956 (223)

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
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GroEL and the GroEL-GroES Complex

2017
Chaperonin is categorized as a molecular chaperone and mediates the formation of the native conformation of proteins by first preventing folding during synthesis or membrane translocation and subsequently by mediating the step-wise ATP-dependent release that result in proper folding.
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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
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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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Thermus thermophilus GroEL, GroES

1997
Abstract Thermus chaperonin means the chaperonin from T. thermophilus, consisting of 14 copies of GroEL homologues (T. th cpn60), seven copies of GroES homologues (T. th cpn10) (Taguchi etal., 1991; Amada etal., 1995).
H Taguchi, M Yoshida
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Urease inactivation by an unusual GroES chaperonin

Science China Chemistry, 2014
It remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model.
Cun, SJ, Sun, H
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Nucleotide sequence of the Escherichia coli groE promoter

Gene, 1994
The promoter region of the Escherichia coli groE operon was cloned using the polymerase chain reaction (PCR). The 118-bp nucleotide sequence of the cloned groE promoter was determined on both strands of DNA. Two bp were found between the -10 and -35 regions of this promoter that have not been reported in previous publications of this sequence.
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Activation of Wheat Defense Response by Buchnera aphidicola-Derived Small Chaperone Protein GroES in Wheat Aphid Saliva

Journal of Agricultural and Food Chemistry, 2022
Qian Li, Maolin Hou, Julian Chen
exaly