The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions
The heat shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is an organism that grows on the gas...
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| Format: | Article |
| Language: | English |
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Elsevier
2017-03-01
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| Series: | Biochemistry and Biophysics Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580816302266 |
| _version_ | 1828793181036085248 |
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| author | Jose A. Mendoza Kevin K. Weinberger Matthew J. Swan |
| author_facet | Jose A. Mendoza Kevin K. Weinberger Matthew J. Swan |
| author_sort | Jose A. Mendoza |
| collection | DOAJ |
| description | The heat shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is an organism that grows on the gastric epithelium, where the pH can fluctuate between neutral and 4.5 and the intracellular pH can be as low as 5.0. This study was performed to test the ability of Hsp60 from H. pylori to function as a molecular chaperone under mildly acidic conditions. We report here that Hsp60 could suppress the acid-induced aggregation of alcohol dehydrogenase (ADH) in the 7.0–5.0 pH range. Hsp60 was found to undergo a conformational change within this pH range. It was also found that exposure of hydrophobic surfaces of Hsp60 is significant and that their exposure is increased under acidic conditions. Although, alcohol dehydrogenase does not contain exposed hydrophobic surfaces, we found that their exposure is triggered at low pH. Our results demonstrate that Hsp60 from H. pylori can function as a molecular chaperone under acidic conditions and that the interaction between Hsp60 and other proteins may be mediated by hydrophobic interactions. |
| first_indexed | 2024-12-12T03:21:30Z |
| format | Article |
| id | doaj.art-7b1bccce9b614f48a1ab51fcc6b141b2 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-12T03:21:30Z |
| publishDate | 2017-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-7b1bccce9b614f48a1ab51fcc6b141b22022-12-22T00:40:09ZengElsevierBiochemistry and Biophysics Reports2405-58082017-03-019C959910.1016/j.bbrep.2016.11.011The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditionsJose A. MendozaKevin K. WeinbergerMatthew J. SwanThe heat shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is an organism that grows on the gastric epithelium, where the pH can fluctuate between neutral and 4.5 and the intracellular pH can be as low as 5.0. This study was performed to test the ability of Hsp60 from H. pylori to function as a molecular chaperone under mildly acidic conditions. We report here that Hsp60 could suppress the acid-induced aggregation of alcohol dehydrogenase (ADH) in the 7.0–5.0 pH range. Hsp60 was found to undergo a conformational change within this pH range. It was also found that exposure of hydrophobic surfaces of Hsp60 is significant and that their exposure is increased under acidic conditions. Although, alcohol dehydrogenase does not contain exposed hydrophobic surfaces, we found that their exposure is triggered at low pH. Our results demonstrate that Hsp60 from H. pylori can function as a molecular chaperone under acidic conditions and that the interaction between Hsp60 and other proteins may be mediated by hydrophobic interactions.http://www.sciencedirect.com/science/article/pii/S2405580816302266Hsp60Molecular chaperoneProtein aggregationAcid stressConformational changes |
| spellingShingle | Jose A. Mendoza Kevin K. Weinberger Matthew J. Swan The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions Biochemistry and Biophysics Reports Hsp60 Molecular chaperone Protein aggregation Acid stress Conformational changes |
| title | The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| title_full | The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| title_fullStr | The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| title_full_unstemmed | The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| title_short | The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| title_sort | hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions |
| topic | Hsp60 Molecular chaperone Protein aggregation Acid stress Conformational changes |
| url | http://www.sciencedirect.com/science/article/pii/S2405580816302266 |
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