Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.
Aminoacyl-tRNA synthetases-interacting multifunctional protein3 (AIMP3/p18) is involved in the macromolecular tRNA synthetase complex via its interaction with several aminoacyl-tRNA synthetases. Recent reports reveal a novel function of AIMP3 as a tumor suppressor by accelerating cellular senescence...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-01-01
|
| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5552228?pdf=render |
| _version_ | 1818193074887589888 |
|---|---|
| author | Yeqing Tao Pengfei Fang Sunghoon Kim Min Guo Nicolas L Young Alan G Marshall |
| author_facet | Yeqing Tao Pengfei Fang Sunghoon Kim Min Guo Nicolas L Young Alan G Marshall |
| author_sort | Yeqing Tao |
| collection | DOAJ |
| description | Aminoacyl-tRNA synthetases-interacting multifunctional protein3 (AIMP3/p18) is involved in the macromolecular tRNA synthetase complex via its interaction with several aminoacyl-tRNA synthetases. Recent reports reveal a novel function of AIMP3 as a tumor suppressor by accelerating cellular senescence and causing defects in nuclear morphology. AIMP3 specifically mediates degradation of mature Lamin A (LmnA), a major component of the nuclear envelope matrix; however, the mechanism of how AIMP3 interacts with LmnA is unclear. Here we report solution-phase hydrogen/deuterium exchange (HDX) for AIMP3, LmnA, and AIMP3 in association with the LmnA C-terminus. Reversed-phase LC coupled with LTQ 14.5 T Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) results in high mass accuracy and resolving power for comparing the D-uptake profiles for AIMP3, LmnA, and their complex. The results show that the AIMP3-LmnA interaction involves one of the two putative binding sites and an adjacent novel interface on AIMP3. LmnA binds AIMP3 via its extreme C-terminus. Together these findings provide a structural insight for understanding the interaction between AIMP3 and LmnA in AIMP3 degradation. |
| first_indexed | 2024-12-12T00:40:37Z |
| format | Article |
| id | doaj.art-f78d4e016a174f5ca4476423b605f71c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T00:40:37Z |
| publishDate | 2017-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-f78d4e016a174f5ca4476423b605f71c2022-12-22T00:44:16ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01128e018186910.1371/journal.pone.0181869Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.Yeqing TaoPengfei FangSunghoon KimMin GuoNicolas L YoungAlan G MarshallAminoacyl-tRNA synthetases-interacting multifunctional protein3 (AIMP3/p18) is involved in the macromolecular tRNA synthetase complex via its interaction with several aminoacyl-tRNA synthetases. Recent reports reveal a novel function of AIMP3 as a tumor suppressor by accelerating cellular senescence and causing defects in nuclear morphology. AIMP3 specifically mediates degradation of mature Lamin A (LmnA), a major component of the nuclear envelope matrix; however, the mechanism of how AIMP3 interacts with LmnA is unclear. Here we report solution-phase hydrogen/deuterium exchange (HDX) for AIMP3, LmnA, and AIMP3 in association with the LmnA C-terminus. Reversed-phase LC coupled with LTQ 14.5 T Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) results in high mass accuracy and resolving power for comparing the D-uptake profiles for AIMP3, LmnA, and their complex. The results show that the AIMP3-LmnA interaction involves one of the two putative binding sites and an adjacent novel interface on AIMP3. LmnA binds AIMP3 via its extreme C-terminus. Together these findings provide a structural insight for understanding the interaction between AIMP3 and LmnA in AIMP3 degradation.http://europepmc.org/articles/PMC5552228?pdf=render |
| spellingShingle | Yeqing Tao Pengfei Fang Sunghoon Kim Min Guo Nicolas L Young Alan G Marshall Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. PLoS ONE |
| title | Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. |
| title_full | Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. |
| title_fullStr | Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. |
| title_full_unstemmed | Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. |
| title_short | Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. |
| title_sort | mapping the contact surfaces in the lamin a aimp3 complex by hydrogen deuterium exchange ft icr mass spectrometry |
| url | http://europepmc.org/articles/PMC5552228?pdf=render |
| work_keys_str_mv | AT yeqingtao mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry AT pengfeifang mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry AT sunghoonkim mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry AT minguo mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry AT nicolaslyoung mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry AT alangmarshall mappingthecontactsurfacesinthelaminaaimp3complexbyhydrogendeuteriumexchangefticrmassspectrometry |