ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking.
Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and op...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3666759?pdf=render |
| _version_ | 1828468122602962944 |
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| author | Hiroshi Sekiguchi Ayumi Nakagawa Kazuki Moriya Koki Makabe Kouhei Ichiyanagi Shunsuke Nozawa Tokushi Sato Shin-ichi Adachi Kunihiro Kuwajima Masafumi Yohda Yuji C Sasaki |
| author_facet | Hiroshi Sekiguchi Ayumi Nakagawa Kazuki Moriya Koki Makabe Kouhei Ichiyanagi Shunsuke Nozawa Tokushi Sato Shin-ichi Adachi Kunihiro Kuwajima Masafumi Yohda Yuji C Sasaki |
| author_sort | Hiroshi Sekiguchi |
| collection | DOAJ |
| description | Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle. Recent structural studies suggest that the ring structure of the chaperonin twists to seal off the central cavity. In this study, we demonstrate ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by diffracted X-ray tracking (DXT). A UV light-triggered DXT study with caged-ATP and stopped-flow fluorometry revealed that the lid partially closed within 1 s of ATP binding, the closed ring subsequently twisted counterclockwise within 2-6 s, as viewed from the top to bottom of the chaperonin, and the twisted ring reverted to the original open-state with a clockwise motion. Our analyses clearly demonstrate that the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion. |
| first_indexed | 2024-12-11T04:17:34Z |
| format | Article |
| id | doaj.art-504a2222ce2447229fc0de1ff7287c72 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T04:17:34Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-504a2222ce2447229fc0de1ff7287c722022-12-22T01:21:12ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0185e6417610.1371/journal.pone.0064176ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking.Hiroshi SekiguchiAyumi NakagawaKazuki MoriyaKoki MakabeKouhei IchiyanagiShunsuke NozawaTokushi SatoShin-ichi AdachiKunihiro KuwajimaMasafumi YohdaYuji C SasakiGroup II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle. Recent structural studies suggest that the ring structure of the chaperonin twists to seal off the central cavity. In this study, we demonstrate ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by diffracted X-ray tracking (DXT). A UV light-triggered DXT study with caged-ATP and stopped-flow fluorometry revealed that the lid partially closed within 1 s of ATP binding, the closed ring subsequently twisted counterclockwise within 2-6 s, as viewed from the top to bottom of the chaperonin, and the twisted ring reverted to the original open-state with a clockwise motion. Our analyses clearly demonstrate that the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion.http://europepmc.org/articles/PMC3666759?pdf=render |
| spellingShingle | Hiroshi Sekiguchi Ayumi Nakagawa Kazuki Moriya Koki Makabe Kouhei Ichiyanagi Shunsuke Nozawa Tokushi Sato Shin-ichi Adachi Kunihiro Kuwajima Masafumi Yohda Yuji C Sasaki ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. PLoS ONE |
| title | ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. |
| title_full | ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. |
| title_fullStr | ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. |
| title_full_unstemmed | ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. |
| title_short | ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. |
| title_sort | atp dependent rotational motion of group ii chaperonin observed by x ray single molecule tracking |
| url | http://europepmc.org/articles/PMC3666759?pdf=render |
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