scholarly journals Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis.

1997 ◽  
Vol 11 (1) ◽  
pp. 119-128 ◽  
Author(s):  
K Turgay ◽  
L W Hamoen ◽  
G Venema ◽  
D Dubnau
Keyword(s):  
Transcription Factor ◽  
Bacillus Subtilis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Molecular Switch

scholarly journals Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain

2015 ◽  
Vol 71 (6) ◽  
pp. 688-696 ◽  
Author(s):  
Swetha Raman ◽  
Kaza Suguna
Keyword(s):  
Crystal Structure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Functional Characterization ◽  
Cell Signalling ◽  
Physiological Role ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle control and in maintaining proteome integrity and protein homeostasis. In plants, Hsp90s are required for normal plant growth and development. Hsp90s are observed to be upregulated in response to various abiotic and biotic stresses and are also involved in immune responses in plants. Although there are several studies elucidating the physiological role of Hsp90s in plants, their molecular mechanism of action is still unclear. In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 fromDictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

Role of heat stress response in the tolerance of immature renal tubules to anoxia

1998 ◽  
Vol 274 (6) ◽  
pp. F1029-F1036 ◽  
Author(s):  
Karen M. Gaudio ◽  
Gunilla Thulin ◽  
Andrea Mann ◽  
Michael Kashgarian ◽  
Norman J. Siegel
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Metabolic Response ◽  
Renal Tubules ◽  
Heat Stress Response

The stress response was studied in suspensions of tubules from immature (IT) and mature (MT) rats after noninjury, heat, oxygen, and anoxia. Under all conditions, IT exhibited more exuberant activation of heat shock transcription factor (HSF) than MT. Characterization of activated HSF in immature cortex revealed HSF1. Also, 2 h after each condition, heat shock protein-72 (HSP-72) mRNA was twofold in IT. As the metabolic response to 45 min of anoxia, 20-min reoxygenation was assessed by measuring O2 consumption (O2C). Basal O2C was manipulated with ouabain, nystatin, and carbonylcyanide p-chloromethyoxyphenylhydrazone (CCCP). Basal O2C in IT were one-half the value of MT. After anoxia, basal O2C was reduced by a greater degree in MT. Ouabain reduced O2C to half the basal value in both noninjured and anoxic groups. Basal O2C was significantly stimulated by nystatin but not to the same level following anoxia in MT and IT. Basal O2C was also stimulated by CCCP, but after anoxia, CCCP O2C was significantly less in MT with no decrease in IT, suggesting mitochondria are better preserved in IT. Also, O2C devoted to nontransport activity was better maintained in IT.

Heat shock protein 60 and adipocytes: Characterization of a ligand-receptor interaction

2010 ◽  
Vol 391 (4) ◽  
pp. 1634-1640 ◽  
Author(s):  
Tina Märker ◽  
Jennifer Kriebel ◽  
Ulrike Wohlrab ◽  
Christiane Habich
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Receptor Interaction ◽  
Heat Shock Protein 60

Biochemical and Biophysical Characterization of the Trimerization Domain from the Heat Shock Transcription Factor†

Biochemistry ◽  
1999 ◽  
Vol 38 (12) ◽  
pp. 3559-3569 ◽  
Author(s):  
Ralph Peteranderl ◽  
Mark Rabenstein ◽  
Yeon-Kyun Shin ◽  
Corey W. Liu ◽  
David E. Wemmer ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Biophysical Characterization

Sequence Characterization of Heat Shock Protein Gene ofCyclospora cayetanensisIsolates from Nepal, Mexico, and Peru

2013 ◽  
Vol 99 (2) ◽  
pp. 379-382 ◽  
Author(s):  
Irshad M. Sulaiman ◽  
Patricia Torres ◽  
Steven Simpson ◽  
Khalil Kerdahi ◽  
Ynes Ortega
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Gene ◽  
Heat Shock Protein Gene ◽  
Sequence Characterization
Sign in / Sign up

Export Citation Format

Share Document