Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33
Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF)...
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2021-11-01
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| author | Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won |
| author_facet | Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won |
| author_sort | Minho Keum |
| collection | DOAJ |
| description | Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions. |
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| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T05:42:14Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
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| spelling | doaj.art-6f6a22656d4b4dc8aa63c07bce5f78722023-11-22T22:28:23ZengMDPI AGBiology2079-77372021-11-011011117110.3390/biology10111171Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33Minho Keum0Dai Ito1Mi-Seong Kim2Yuxi Lin3Kyeong-Hyeon Yoon4Jihoon Kim5Sung-Hee Lee6Ji-Hun Kim7Wookyung Yu8Young-Ho Lee9Hyung-Sik Won10Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, KoreaDepartment of Brain and Cognitive Sciences, DGIST, Daegu 42988, KoreaDepartment of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, KoreaResearch Center of Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Cheongju 28119, KoreaDepartment of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, KoreaDepartment of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, KoreaCollege of Pharmacy, Chungbuk National University, Cheongju 28160, KoreaCollege of Pharmacy, Chungbuk National University, Cheongju 28160, KoreaDepartment of Brain and Cognitive Sciences, DGIST, Daegu 42988, KoreaResearch Center of Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Cheongju 28119, KoreaDepartment of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, KoreaHsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions.https://www.mdpi.com/2079-7737/10/11/1171aggregase activityEF-TuEF-TsproteostasisHsp33molecular chaperone |
| spellingShingle | Minho Keum Dai Ito Mi-Seong Kim Yuxi Lin Kyeong-Hyeon Yoon Jihoon Kim Sung-Hee Lee Ji-Hun Kim Wookyung Yu Young-Ho Lee Hyung-Sik Won Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 Biology aggregase activity EF-Tu EF-Ts proteostasis Hsp33 molecular chaperone |
| title | Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 |
| title_full | Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 |
| title_fullStr | Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 |
| title_full_unstemmed | Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 |
| title_short | Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33 |
| title_sort | molecular effects of elongation factor ts and trigger factor on the unfolding and aggregation of elongation factor tu induced by the prokaryotic molecular chaperone hsp33 |
| topic | aggregase activity EF-Tu EF-Ts proteostasis Hsp33 molecular chaperone |
| url | https://www.mdpi.com/2079-7737/10/11/1171 |
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