Processivity of dimeric kinesin‐1 molecular motors
Kinesin‐1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we computationally studied the run length of the dimer with...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2018-08-01
|
| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/2211-5463.12486 |
| _version_ | 1827397854866440192 |
|---|---|
| author | Si‐Kao Guo Xiao‐Xuan Shi Peng‐Ye Wang Ping Xie |
| author_facet | Si‐Kao Guo Xiao‐Xuan Shi Peng‐Ye Wang Ping Xie |
| author_sort | Si‐Kao Guo |
| collection | DOAJ |
| description | Kinesin‐1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we computationally studied the run length of the dimer with our proposed model. The computational data quantitatively reproduced the puzzling experimental data, including the dramatically asymmetric character of the run length with respect to the direction of external load acting on the coiled‐coil stalk, the enhancement of the run length by addition of phosphate, and the contrary features of the run length for different types of kinesin‐1 with extensions of their neck linkers compared with those without extension of the neck linker. The computational data on other aspects of the movement dynamics such as velocity and durations of one‐head‐bound and two‐head‐bound states in a mechanochemical coupling cycle were also in quantitative agreement with the available experimental data. Moreover, predicted results are provided on dependence of the run length upon external load acting on one head of the dimer, which can be easily tested in the future using single‐molecule optical trapping assays. |
| first_indexed | 2024-03-08T19:17:52Z |
| format | Article |
| id | doaj.art-bc1edc7c63b9441e9b178f5b7260b713 |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-03-08T19:17:52Z |
| publishDate | 2018-08-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-bc1edc7c63b9441e9b178f5b7260b7132023-12-27T04:21:38ZengWileyFEBS Open Bio2211-54632018-08-01881332135110.1002/2211-5463.12486Processivity of dimeric kinesin‐1 molecular motorsSi‐Kao Guo0Xiao‐Xuan Shi1Peng‐Ye Wang2Ping Xie3Key Laboratory of Soft Matter Physics Beijing National Laboratory for Condensed Matter Physics Institute of Physics Chinese Academy of Science Beijing ChinaKey Laboratory of Soft Matter Physics Beijing National Laboratory for Condensed Matter Physics Institute of Physics Chinese Academy of Science Beijing ChinaKey Laboratory of Soft Matter Physics Beijing National Laboratory for Condensed Matter Physics Institute of Physics Chinese Academy of Science Beijing ChinaKey Laboratory of Soft Matter Physics Beijing National Laboratory for Condensed Matter Physics Institute of Physics Chinese Academy of Science Beijing ChinaKinesin‐1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we computationally studied the run length of the dimer with our proposed model. The computational data quantitatively reproduced the puzzling experimental data, including the dramatically asymmetric character of the run length with respect to the direction of external load acting on the coiled‐coil stalk, the enhancement of the run length by addition of phosphate, and the contrary features of the run length for different types of kinesin‐1 with extensions of their neck linkers compared with those without extension of the neck linker. The computational data on other aspects of the movement dynamics such as velocity and durations of one‐head‐bound and two‐head‐bound states in a mechanochemical coupling cycle were also in quantitative agreement with the available experimental data. Moreover, predicted results are provided on dependence of the run length upon external load acting on one head of the dimer, which can be easily tested in the future using single‐molecule optical trapping assays.https://doi.org/10.1002/2211-5463.12486coordinationkinesinmechanochemical couplingmolecular motorrun length |
| spellingShingle | Si‐Kao Guo Xiao‐Xuan Shi Peng‐Ye Wang Ping Xie Processivity of dimeric kinesin‐1 molecular motors FEBS Open Bio coordination kinesin mechanochemical coupling molecular motor run length |
| title | Processivity of dimeric kinesin‐1 molecular motors |
| title_full | Processivity of dimeric kinesin‐1 molecular motors |
| title_fullStr | Processivity of dimeric kinesin‐1 molecular motors |
| title_full_unstemmed | Processivity of dimeric kinesin‐1 molecular motors |
| title_short | Processivity of dimeric kinesin‐1 molecular motors |
| title_sort | processivity of dimeric kinesin 1 molecular motors |
| topic | coordination kinesin mechanochemical coupling molecular motor run length |
| url | https://doi.org/10.1002/2211-5463.12486 |
| work_keys_str_mv | AT sikaoguo processivityofdimerickinesin1molecularmotors AT xiaoxuanshi processivityofdimerickinesin1molecularmotors AT pengyewang processivityofdimerickinesin1molecularmotors AT pingxie processivityofdimerickinesin1molecularmotors |