Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX
Abstract RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO2 in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series of chaperones that include RbcX and RuBisCO accumulation factor 1 (Raf1). To understand ho...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2022-09-01
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| Series: | Cell Discovery |
| Online Access: | https://doi.org/10.1038/s41421-022-00436-9 |
| _version_ | 1828111736964644864 |
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| author | Qiong Li Yong-Liang Jiang Ling-Yun Xia Yuxing Chen Cong-Zhao Zhou |
| author_facet | Qiong Li Yong-Liang Jiang Ling-Yun Xia Yuxing Chen Cong-Zhao Zhou |
| author_sort | Qiong Li |
| collection | DOAJ |
| description | Abstract RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO2 in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series of chaperones that include RbcX and RuBisCO accumulation factor 1 (Raf1). To understand how these RuBisCO-specific chaperones function during cyanobacterial RbcL8RbcS8 (L8S8) holoenzyme formation, we solved a 3.3-Å cryo-electron microscopy structure of a 32-subunit RbcL8Raf18RbcX16 (L8F8X16) assembly intermediate from Anabaena sp. PCC 7120. Comparison to the previously resolved L8F8 and L8X16 structures together with biochemical assays revealed that the L8F8X16 complex forms a rather dynamic structural intermediate, favoring RbcS displacement of Raf1 and RbcX. In vitro assays further demonstrated that both Raf1 and RbcX function to regulate RuBisCO condensate formation by restricting CcmM35 binding to the stably assembled L8S8 holoenzymes. Combined with previous findings, we propose a model on how Raf1 and RbcX work in concert to facilitate, and regulate, cyanobacterial RuBisCO assembly as well as disassembly of RuBisCO condensates. |
| first_indexed | 2024-04-11T11:40:08Z |
| format | Article |
| id | doaj.art-6ca559d71e4e4c5681fa25a633f93e62 |
| institution | Directory Open Access Journal |
| issn | 2056-5968 |
| language | English |
| last_indexed | 2024-04-11T11:40:08Z |
| publishDate | 2022-09-01 |
| publisher | Nature Publishing Group |
| record_format | Article |
| series | Cell Discovery |
| spelling | doaj.art-6ca559d71e4e4c5681fa25a633f93e622022-12-22T04:25:52ZengNature Publishing GroupCell Discovery2056-59682022-09-018111110.1038/s41421-022-00436-9Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcXQiong Li0Yong-Liang Jiang1Ling-Yun Xia2Yuxing Chen3Cong-Zhao Zhou4School of Life Sciences, University of Science and Technology of ChinaSchool of Life Sciences, University of Science and Technology of ChinaSchool of Life Sciences, University of Science and Technology of ChinaSchool of Life Sciences, University of Science and Technology of ChinaSchool of Life Sciences, University of Science and Technology of ChinaAbstract RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO2 in photosynthesis. Its common form consists of eight RbcL and eight RbcS subunits, the assembly of which requires a series of chaperones that include RbcX and RuBisCO accumulation factor 1 (Raf1). To understand how these RuBisCO-specific chaperones function during cyanobacterial RbcL8RbcS8 (L8S8) holoenzyme formation, we solved a 3.3-Å cryo-electron microscopy structure of a 32-subunit RbcL8Raf18RbcX16 (L8F8X16) assembly intermediate from Anabaena sp. PCC 7120. Comparison to the previously resolved L8F8 and L8X16 structures together with biochemical assays revealed that the L8F8X16 complex forms a rather dynamic structural intermediate, favoring RbcS displacement of Raf1 and RbcX. In vitro assays further demonstrated that both Raf1 and RbcX function to regulate RuBisCO condensate formation by restricting CcmM35 binding to the stably assembled L8S8 holoenzymes. Combined with previous findings, we propose a model on how Raf1 and RbcX work in concert to facilitate, and regulate, cyanobacterial RuBisCO assembly as well as disassembly of RuBisCO condensates.https://doi.org/10.1038/s41421-022-00436-9 |
| spellingShingle | Qiong Li Yong-Liang Jiang Ling-Yun Xia Yuxing Chen Cong-Zhao Zhou Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX Cell Discovery |
| title | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX |
| title_full | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX |
| title_fullStr | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX |
| title_full_unstemmed | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX |
| title_short | Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX |
| title_sort | structural insights into cyanobacterial rubisco assembly coordinated by two chaperones raf1 and rbcx |
| url | https://doi.org/10.1038/s41421-022-00436-9 |
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