Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB
The acid stress chaperones HdeA and HdeB of Escherichia coli prevent the aggregation of periplasmic proteins at acidic pH. We show in this report that they also form mixed aggregates with proteins that have failed to be solubilized at acidic pH and allow their subsequent solubilization at neutral pH...
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2008
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| Online Access: | http://hdl.handle.net/10725/4162 http://dx.doi.org/ doi: 10.1074/jbc.M800869200 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://www.jbc.org/content/283/20/13679.short |
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| _version_ | 1864513462927884288 |
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| author | Malki, Abderrahim |
| author2 | Le, Hai-Tuong Milles, Sigrid Kern, Renee Caldas, Teresa Abdallah, Jad Richarme, Gilbert |
| author2_role | author author author author author author |
| author_facet | Malki, Abderrahim Le, Hai-Tuong Milles, Sigrid Kern, Renee Caldas, Teresa Abdallah, Jad Richarme, Gilbert |
| author_role | author |
| dc.creator.none.fl_str_mv | Malki, Abderrahim Le, Hai-Tuong Milles, Sigrid Kern, Renee Caldas, Teresa Abdallah, Jad Richarme, Gilbert |
| dc.date.none.fl_str_mv | 2008 2016-07-19T08:31:02Z 2016-07-19T08:31:02Z 2016-07-19 |
| dc.identifier.none.fl_str_mv | 1431-6730 http://hdl.handle.net/10725/4162 http://dx.doi.org/ doi: 10.1074/jbc.M800869200 Malki, A., Le, H. T., Milles, S., Kern, R., Caldas, T., Abdallah, J., & Richarme, G. (2008). Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. Journal of Biological Chemistry, 283(20), 13679-13687. http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://www.jbc.org/content/283/20/13679.short |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | The Journal of Biological Chemistry |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | The acid stress chaperones HdeA and HdeB of Escherichia coli prevent the aggregation of periplasmic proteins at acidic pH. We show in this report that they also form mixed aggregates with proteins that have failed to be solubilized at acidic pH and allow their subsequent solubilization at neutral pH. HdeA, HdeB, and HdeA and HdeB together display an increasing efficiency for the solubilization of protein aggregates at pH 3. They are less efficient for the solubilization of aggregates at pH 2, whereas HdeB is the most efficient. Increasing amounts of periplasmic proteins draw increasing amounts of chaperone into pellets, suggesting that chaperones co-aggregate with their substrate proteins. We observed a decrease in the size of protein aggregates in the presence of HdeA and HdeB, from very high molecular mass aggregates to 100–5000-kDa species. Moreover, a marked decrease in the exposed hydrophobicity of aggregated proteins in the presence of HdeA and HdeB was revealed by 1,1′-bis(4-anilino)naphtalene-5,5′-disulfonic acid binding experiments. In vivo, during the recovery at neutral pH of acid stressed bacterial cells, HdeA and HdeB allow the solubilization and renaturation of protein aggregates, including those formed by the maltose receptor MalE, the oligopeptide receptor OppA, and the histidine receptor HisJ. Thus, HdeA and HdeB not only help to maintain proteins in a soluble state during acid treatment, as previously reported, but also assist, both in vitro and in vivo, in the solubilization at neutral pH of mixed protein-chaperone aggregates formed at acidic pH, by decreasing the size of protein aggregates and the exposed hydrophobicity of aggregated proteins. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_05497c759cba3e516cce8d5f6598fdfa |
| identifier_str_mv | 1431-6730 Malki, A., Le, H. T., Milles, S., Kern, R., Caldas, T., Abdallah, J., & Richarme, G. (2008). Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. Journal of Biological Chemistry, 283(20), 13679-13687. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/4162 |
| publishDate | 2008 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeBMalki, AbderrahimLe, Hai-TuongMilles, SigridKern, ReneeCaldas, TeresaAbdallah, JadRicharme, GilbertThe acid stress chaperones HdeA and HdeB of Escherichia coli prevent the aggregation of periplasmic proteins at acidic pH. We show in this report that they also form mixed aggregates with proteins that have failed to be solubilized at acidic pH and allow their subsequent solubilization at neutral pH. HdeA, HdeB, and HdeA and HdeB together display an increasing efficiency for the solubilization of protein aggregates at pH 3. They are less efficient for the solubilization of aggregates at pH 2, whereas HdeB is the most efficient. Increasing amounts of periplasmic proteins draw increasing amounts of chaperone into pellets, suggesting that chaperones co-aggregate with their substrate proteins. We observed a decrease in the size of protein aggregates in the presence of HdeA and HdeB, from very high molecular mass aggregates to 100–5000-kDa species. Moreover, a marked decrease in the exposed hydrophobicity of aggregated proteins in the presence of HdeA and HdeB was revealed by 1,1′-bis(4-anilino)naphtalene-5,5′-disulfonic acid binding experiments. In vivo, during the recovery at neutral pH of acid stressed bacterial cells, HdeA and HdeB allow the solubilization and renaturation of protein aggregates, including those formed by the maltose receptor MalE, the oligopeptide receptor OppA, and the histidine receptor HisJ. Thus, HdeA and HdeB not only help to maintain proteins in a soluble state during acid treatment, as previously reported, but also assist, both in vitro and in vivo, in the solubilization at neutral pH of mixed protein-chaperone aggregates formed at acidic pH, by decreasing the size of protein aggregates and the exposed hydrophobicity of aggregated proteins.PublishedN/A2016-07-19T08:31:02Z2016-07-19T08:31:02Z20082016-07-19Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1431-6730http://hdl.handle.net/10725/4162http://dx.doi.org/ doi: 10.1074/jbc.M800869200Malki, A., Le, H. T., Milles, S., Kern, R., Caldas, T., Abdallah, J., & Richarme, G. (2008). Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. Journal of Biological Chemistry, 283(20), 13679-13687.http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.phphttp://www.jbc.org/content/283/20/13679.shortenThe Journal of Biological Chemistryinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/41622021-03-19T10:03:23Z |
| spellingShingle | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB Malki, Abderrahim |
| status_str | publishedVersion |
| title | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| title_full | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| title_fullStr | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| title_full_unstemmed | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| title_short | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| title_sort | Solubilization of Protein Aggregates by the Acid Stress Chaperones HdeA and HdeB |
| url | http://hdl.handle.net/10725/4162 http://dx.doi.org/ doi: 10.1074/jbc.M800869200 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://www.jbc.org/content/283/20/13679.short |