Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
<i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-10-01
|
| Series: | Biology |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-7737/10/11/1106 |
| _version_ | 1797511228579381248 |
|---|---|
| author | Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio |
| author_facet | Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio |
| author_sort | Haojie Zhu |
| collection | DOAJ |
| description | <i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of <i>Tt</i>TF in the absence and presence of Zn<sup>2+</sup>. The data show that full-length <i>Tt</i>TF binds Zn<sup>2+</sup>, but the isolated domains and tandem domains of <i>Tt</i>TF do not bind to Zn<sup>2+</sup>. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn<sup>2+</sup>-binding induces the partial structural changes of <i>Tt</i>TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn<sup>2+</sup> promotes <i>Tt</i>TF oligomerization. Given the previous work showing that the activity regulation of <i>E. coli</i> trigger factor is accompanied by oligomerization, the data suggest that <i>Tt</i>TF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment. |
| first_indexed | 2024-03-10T05:42:23Z |
| format | Article |
| id | doaj.art-9387f760265d4623b412e62eef8a4b08 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T05:42:23Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-9387f760265d4623b412e62eef8a4b082023-11-22T22:27:26ZengMDPI AGBiology2079-77372021-10-011011110610.3390/biology10111106Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor ChaperoneHaojie Zhu0Motonori Matsusaki1Taiga Sugawara2Koichiro Ishimori3Tomohide Saio4Institute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, JapanInstitute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, JapanGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-8628, JapanGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-8628, JapanInstitute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, Japan<i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of <i>Tt</i>TF in the absence and presence of Zn<sup>2+</sup>. The data show that full-length <i>Tt</i>TF binds Zn<sup>2+</sup>, but the isolated domains and tandem domains of <i>Tt</i>TF do not bind to Zn<sup>2+</sup>. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn<sup>2+</sup>-binding induces the partial structural changes of <i>Tt</i>TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn<sup>2+</sup> promotes <i>Tt</i>TF oligomerization. Given the previous work showing that the activity regulation of <i>E. coli</i> trigger factor is accompanied by oligomerization, the data suggest that <i>Tt</i>TF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment.https://www.mdpi.com/2079-7737/10/11/1106trigger factorzinc-dependent chaperone<i>Thermus thermophilus</i>thermal stabilitysecondary structuremass spectrometry |
| spellingShingle | Haojie Zhu Motonori Matsusaki Taiga Sugawara Koichiro Ishimori Tomohide Saio Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone Biology trigger factor zinc-dependent chaperone <i>Thermus thermophilus</i> thermal stability secondary structure mass spectrometry |
| title | Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone |
| title_full | Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone |
| title_fullStr | Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone |
| title_full_unstemmed | Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone |
| title_short | Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone |
| title_sort | zinc dependent oligomerization of i thermus thermophilus i trigger factor chaperone |
| topic | trigger factor zinc-dependent chaperone <i>Thermus thermophilus</i> thermal stability secondary structure mass spectrometry |
| url | https://www.mdpi.com/2079-7737/10/11/1106 |
| work_keys_str_mv | AT haojiezhu zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT motonorimatsusaki zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT taigasugawara zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT koichiroishimori zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone AT tomohidesaio zincdependentoligomerizationofithermusthermophilusitriggerfactorchaperone |