Results 151 to 160 of about 9,153 (190)
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Structure and function of the GroE chaperone
Cellular and Molecular Life Sciences, 2002The 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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Reversible Oligomerization and Denaturation of the Chaperonin GroES
Biochemistry, 1996The 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 +3 more
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NMR analysis of a 900K GroEL–GroES complex
Nature, 2002Biomacromolecular structures with a relative molecular mass (M(r)) of 50,000 to 100,000 (50K 100K) have been generally considered to be inaccessible to analysis by solution NMR spectroscopy. Here we report spectra recorded from bacterial chaperonin complexes ten times this size limit (up to M(r) 900K) using the techniques of transverse relaxation ...
Fiaux J +3 more
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The GroES antigens of Mycobacterium avium and Mycobacterium paratuberculosis
Veterinary Microbiology, 1999The GroES antigen provokes a strong immune response in human beings with tuberculosis or leprosy. We cloned and sequenced the Mycobacterium avium and Mycobacterium paratuberculosis GroES genes. M. avium and M. paratuberculosis have identical GroES sequences which differ from other mycobacterial species. This supports the current formal designation of M.
A J, Cobb, R, Frothingham
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GroEL and the GroEL-GroES Complex
2017Chaperonin 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, 1997For 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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Characterization of a functionally important mobile domain of GroES
Nature, 1993Although genetic and biochemical evidence has established that GroES is required for the full function of the molecular chaperone, GroEL, little is known about the molecular details of their interaction. GroES enhances the cooperativity of ATP binding and hydrolysis by GroEL (refs 4, 5) and is necessary for release and folding of several GroEL ...
S J, Landry +4 more
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Preformed GroES Oligomers Are Not Required as Functional Cochaperonins
Journal of Protein Chemistry, 1997We have previously shown that the C-terminal sequence of GroES is required for oligomerization [Seale and Horowitz (1995), J. Biol. Chem. 270, 30268-30270]. In this report, we have generated a C-terminal deletion mutant of GroES with a significantly destabilized oligomer and have investigated its function in the chaperonin-assisted protein folding ...
J W, Seale +3 more
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Evaluation of the stability of an SR398/GroES chaperonin complex
The Journal of Biochemistry, 2014The stability of an SR398/GroES chaperonin complex was examined. As was expected, based on the finding of previous studies, the SR398/GroES complex was extremely stable in the presence of an excess amount of free adenosine 5'-[γ-thio]triphosphate (ATPγS) or adenosine 5'-(β,γ-imido)triphosphate (AMPPNP).
So, Ishino +4 more
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GroE-mediated folding of bacterial luciferases in vivo
Molecular and General Genetics MGG, 1993In 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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