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Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.

Title: Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry.
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Name(s): Tao, Yeqing, author
Fang, Pengfei, author
Kim, Sunghoon, author
Guo, Min, author
Young, Nicolas L, author
Marshall, Alan G, author
Type of Resource: text
Genre: Journal Article
Text
Date Issued: 2017-08-10
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/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.
Identifier: FSU_pmch_28797100 (IID), 10.1371/journal.pone.0181869 (DOI), PMC5552228 (PMCID), 28797100 (RID), 28797100 (EID), PONE-D-17-10096 (PII)
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5552228.
Subject(s): Amino Acid Sequence
Binding Sites
Deuterium Exchange Measurement/methods
Humans
Lamin Type A/chemistry
Lamin Type A/metabolism
Mass Spectrometry/methods
Molecular Docking Simulation
Peptide Elongation Factors/chemistry
Peptide Elongation Factors/metabolism
Protein Binding
Protein Interaction Mapping
Protein Interaction Maps
Proteolysis
Tumor Suppressor Proteins/chemistry
Tumor Suppressor Proteins/metabolism
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_pmch_28797100
Owner Institution: FSU
Is Part Of: PloS one.
1932-6203
Issue: iss. 8, vol. 12

Choose the citation style.
Tao, Y., Fang, P., Kim, S., Guo, M., Young, N. L., & Marshall, A. G. (2017). Mapping the contact surfaces in the Lamin A:AIMP3 complex by hydrogen/deuterium exchange FT-ICR mass spectrometry. Plos One. Retrieved from http://purl.flvc.org/fsu/fd/FSU_pmch_28797100