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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lo, Hui-Fen Chen, Bo-En Lin, Min-Guan Chi, Meng-Chun Wang, Tzu-Fan Lin, Long-Liu |
| Description | Country affiliation: Taiwan Author Affiliation: Lo HF ( Department of Food Science and Technology, Hungkuang University, 1018 Taiwan Boulevard, Shalu District, Taichung 43302, Taiwan.); Chen BE ( Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi 60004, Taiwan.); Lin MG ( Institute of Molecular Biology, Academia Sinica, Nangang District, Taipei 11529, Taiwan.); Chi MC ( Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi 60004, Taiwan.); Wang TF ( Department of Chemistry, National Cheng Kung University, Tainan 701, Taiwan. Electronic address: catalpa0905@gmail.com.); Lin LL ( Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi 60004, Taiwan. Electronic address: llin@mail.ncyu.edu.tw.) |
| Abstract | Heat shock protein 90 (Hsp90/HtpG) is a highly abundant and ubiquitous ATP-dependent molecular chaperone consisting of three flexibly linked regions, an N-terminal nucleotide-binding domain, middle domain, and a C-terminal domain. Here the putative htpG gene of Bacillus licheniformis was cloned and heterologously expressed in Escherichia coli M15 cells. Native-gel electrophoresis, size exclusion chromatography, and cross-linking analysis revealed that the recombinant protein probably exists as a mixture of monomer, dimer and other oligomers in solution. The optimal conditions for the ATPase activity of B. licheniformis HtpG (BlHtpG) were 45°C and pH 7.0 in the presence of 0.5mM Mg(2+) ions. The molecular architecture of this protein was stable at higher temperatures with a transition point (Tm) of 45°C at neutral pH, whereas the Tm value was reduced to 40.8°C at pH 10.5. Acrylamide quenching experiment further indicated that the dynamic quenching constant (Ksv) of BlHtpG became larger at higher pH values. BlHtpG also experienced a significant change in the protein conformation upon the addition of ATP and organic solvents. Collectively, our experiment data may provide insights into the molecular properties of BlHtpG and identify the alteration of protein structure to forfeit the ATPase activity at alkaline conditions. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 85 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Bacillus Genetics Bacterial Proteins Metabolism Gene Expression Hsp90 Heat-shock Proteins Adenosine Triphosphate Chemistry Amino Acid Sequence Classification Isolation & Purification Enzyme Activation Hydrogen-ion Concentration Molecular Sequence Data Phylogeny Protein Conformation Recombinant Fusion Proteins Sequence Alignment Sequence Analysis, Dna Spectrophotometry, Ultraviolet Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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