Chlamydial GroEL Autoregulates Its Own Expression through Direct Interactions with the HrcA Repressor Protein

Autor: Adam C. Wilson, John R. Yates, Christine C. Wu, Ming Tan

Publikováno v: Wilson, Adam C; Wu, Christine C; Yates, John R; & Tan, Ming. (2005). Chlamydial GroEL autoregulates its own expression through direct interactions with the HrcA repressor protein.. Journal of Bacteriology, 187(21), 7535-7542. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/5p65m7cn

In the pathogenic bacterium Chlamydia trachomatis , a transcriptional repressor, HrcA, regulates the major heat shock operons, dnaK and groE . Cellular stress causes a transient increase in transcription of these heat shock operons through relief of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ce6001228f607f42d18ae86bc5c8241
https://doi.org/10.1128/jb.187.21.7535-7542.2005

Structural Stability of Oligomeric Chaperonin 10: the Role of Two β-Strands at the N and C Termini in Structural Stabilization

Autor: Chiduru Matsumoto, Katsuaki Inoue, Mitsuyoshi Ikeda, Takashi Higurashi, Kunihiro Hongo, Yasushi Kawata, Isao Sakane, Tomohiro Mizobata

Publikováno v: Journal of Molecular Biology. 344:1123-1133

Chaperonin 10 (cpn10) is a well-conserved subgroup of the molecular chaperone family. GroES, the cpn10 from Escherichia coli, is composed of seven 10kDa subunits, which form a dome-like oligomeric ring structure. From our previous studies, it was fou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e02ccce4f1c7acd5cebd9599188e3fb3
https://doi.org/10.1016/j.jmb.2004.09.082

Bordetella pertussis Proteins Dominating the Major Histocompatibility Complex Class II-Presented Epitope Repertoire in Human Monocyte-Derived Dendritic Cells

Autor: Cécile A. C. M. van Els, Martien C. M. Poelen, Rachel M. Stenger, Claire J. P. Boog, Ad P. J. M. de Jong, Hugo D. Meiring, Betsy Kuipers, Jacqueline A. M. van Gaans-van den Brink

Knowledge of naturally processed Bordetella pertussis -specific T cell epitopes may help to increase our understanding of the basis of cell-mediated immune mechanisms to control this reemerging pathogen. Here, we elucidate for the first time the domi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a5e737651b8cca46c2907b5789af93c
https://europepmc.org/articles/PMC4018886/

The Lower Hydrolysis of ATP by the Stress Protein GroEL Is a Major Factor Responsible for the Diminished Chaperonin Activity at Low Temperature

Autor: Pam Dulin, Jose A. Mendoza, Terri Warren

Publikováno v: Cryobiology. 41:319-323

The chaperonins GroEL and GroES were shown to facilitate the refolding of urea-unfolded rhodanese in an ATP-dependent process at 25 or 37 degrees C. A diminished chaperonin activity was observed at 10 degrees C, however. At low temperature, GroEL ret

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e1dfc36b21afa11e34538477e13f8de
https://doi.org/10.1006/cryo.2000.2287

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

Autor: Frank Weber, France Keppel, Costa Georgopoulos, Manajit K. Hayer-Hartl, F. Ulrich Hartl

Publikováno v: Nature Structural Biology. 5:977-985

Two models are being considered for the mechanism of chaperonin-assisted protein folding in E. coli: (i) GroEL/GroES act primarily by enclosing substrate polypeptide in a folding cage in which aggregation is prevented during folding. (ii) GroEL media

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05730737c621828ba19cdc3ebf424c71
https://doi.org/10.1038/2952