Conformational Changes of α-Crystallin Proteins Induced by Heat Stress
α-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of two relative subunits, αA and αB crystallin, which function in maintaining lens transparency. As a member of the small heat-shock protein family (sHsp), α-crystallin exhibits chaperone-like activity to pr...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-08-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/23/16/9347 |
| _version_ | 1797409710274510848 |
|---|---|
| author | Yu-Yung Chang Meng-Hsuan Hsieh Yen-Chieh Huang Chun-Jung Chen Ming-Tao Lee |
| author_facet | Yu-Yung Chang Meng-Hsuan Hsieh Yen-Chieh Huang Chun-Jung Chen Ming-Tao Lee |
| author_sort | Yu-Yung Chang |
| collection | DOAJ |
| description | α-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of two relative subunits, αA and αB crystallin, which function in maintaining lens transparency. As a member of the small heat-shock protein family (sHsp), α-crystallin exhibits chaperone-like activity to prevent the misfolding or aggregation of critical proteins in the lens, which is associated with cataract disease. In this study, high-purity αA and αB crystallin proteins were expressed from <i>E. coli</i> and purified by affinity and size-exclusion chromatography. The size-exclusion chromatography experiment showed that both αA and αB crystallins exhibited oligomeric complexes in solution. Here, we present the structural characteristics of α-crystallin proteins from low to high temperature by combining circular dichroism (CD) and small-angle X-ray scattering (SAXS). Not only the CD data, but also SAXS data show that α-crystallin proteins exhibit transition behavior on conformation with temperature increasing. Although their protein sequences are highly conserved, the analysis of their thermal stability showed different properties in αA and αB crystallin. In this study, taken together, the data discussed were provided to demonstrate more insights into the chaperone-like activity of α-crystallin proteins. |
| first_indexed | 2024-03-09T04:19:33Z |
| format | Article |
| id | doaj.art-f68eef0ea7ab440bbed91b9f0262c34d |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T04:19:33Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-f68eef0ea7ab440bbed91b9f0262c34d2023-12-03T13:49:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-08-012316934710.3390/ijms23169347Conformational Changes of α-Crystallin Proteins Induced by Heat StressYu-Yung Chang0Meng-Hsuan Hsieh1Yen-Chieh Huang2Chun-Jung Chen3Ming-Tao Lee4Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, TaiwanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, TaiwanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, TaiwanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, TaiwanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwanα-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of two relative subunits, αA and αB crystallin, which function in maintaining lens transparency. As a member of the small heat-shock protein family (sHsp), α-crystallin exhibits chaperone-like activity to prevent the misfolding or aggregation of critical proteins in the lens, which is associated with cataract disease. In this study, high-purity αA and αB crystallin proteins were expressed from <i>E. coli</i> and purified by affinity and size-exclusion chromatography. The size-exclusion chromatography experiment showed that both αA and αB crystallins exhibited oligomeric complexes in solution. Here, we present the structural characteristics of α-crystallin proteins from low to high temperature by combining circular dichroism (CD) and small-angle X-ray scattering (SAXS). Not only the CD data, but also SAXS data show that α-crystallin proteins exhibit transition behavior on conformation with temperature increasing. Although their protein sequences are highly conserved, the analysis of their thermal stability showed different properties in αA and αB crystallin. In this study, taken together, the data discussed were provided to demonstrate more insights into the chaperone-like activity of α-crystallin proteins.https://www.mdpi.com/1422-0067/23/16/9347α-crystallinchaperone activitycircular dichroismsmall-angle X-ray scattering |
| spellingShingle | Yu-Yung Chang Meng-Hsuan Hsieh Yen-Chieh Huang Chun-Jung Chen Ming-Tao Lee Conformational Changes of α-Crystallin Proteins Induced by Heat Stress International Journal of Molecular Sciences α-crystallin chaperone activity circular dichroism small-angle X-ray scattering |
| title | Conformational Changes of α-Crystallin Proteins Induced by Heat Stress |
| title_full | Conformational Changes of α-Crystallin Proteins Induced by Heat Stress |
| title_fullStr | Conformational Changes of α-Crystallin Proteins Induced by Heat Stress |
| title_full_unstemmed | Conformational Changes of α-Crystallin Proteins Induced by Heat Stress |
| title_short | Conformational Changes of α-Crystallin Proteins Induced by Heat Stress |
| title_sort | conformational changes of α crystallin proteins induced by heat stress |
| topic | α-crystallin chaperone activity circular dichroism small-angle X-ray scattering |
| url | https://www.mdpi.com/1422-0067/23/16/9347 |
| work_keys_str_mv | AT yuyungchang conformationalchangesofacrystallinproteinsinducedbyheatstress AT menghsuanhsieh conformationalchangesofacrystallinproteinsinducedbyheatstress AT yenchiehhuang conformationalchangesofacrystallinproteinsinducedbyheatstress AT chunjungchen conformationalchangesofacrystallinproteinsinducedbyheatstress AT mingtaolee conformationalchangesofacrystallinproteinsinducedbyheatstress |