Cited by 2Mass Spectrometry Techniques and ApplicationsAdvanced Proteomics Techniques and ApplicationsProtein Structure and Dynamics

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

Open access
Luo, Jie, Ranish, Jeff·2024·eLife

Published version of a preprint

Abstract

Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. Here, we introduce a novel isobaric crosslinker, Qlinker, for studying conformational and structural changes in proteins and protein complexes using quantitative crosslinking mass spectrometry. Qlinkers are small and simple, amine-reactive molecules with an optimal extended distance of ~10 Å, which use MS2 reporter ions for relative quantification of Qlinker-modified peptides derived from different samples. We synthesized the 2-plex Q2linker and showed that the Q2linker can provide quantitative crosslinking data that pinpoints key conformational and structural changes in biosensors, binary and ternary complexes composed of the general transcription factors TBP, TFIIA, and TFIIB, and RNA polymerase II complexes.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.7554/elife.99809.3

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 3 references

Research works printed but not linked: 77

  1. Abdella, 2021, Structure of the human Mediator-bound transcription preinitiation complex, Science, 372, 52, 10.1126/science.abg3074 · DOI
  2. Akey, 2022, Comprehensive structure and functional adaptations of the yeast nuclear pore complex, Cell, 185, 361, 10.1016/j.cell.2021.12.015 · DOI · Paper page
  3. Andel, 1999, Three-dimensional structure of the human TFIID-IIA-IIB complex, Science, 286, 2153, 10.1126/science.286.5447.2153 · DOI
  4. Bangur, 1999, An interaction between the N-terminal region and the core domain of yeast TFIIB promotes the formation of TATA-binding protein-TFIIB-DNA complexes, The Journal of Biological Chemistry, 274, 23203, 10.1074/jbc.274.33.23203 · DOI
  5. Bleichenbacher, 2003, Novel interactions between the components of human and yeast TFIIA/TBP/DNA complexes, Journal of Molecular Biology, 332, 783, 10.1016/s0022-2836(03)00887-8 · DOI
  6. Burger, 2016, A structure-free method for quantifying conformational flexibility in proteins, Scientific Reports, 6, 10.1038/srep29040 · DOI
  7. Bushnell, 2003, Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications for the initiation of transcription, PNAS, 100, 6969, 10.1073/pnas.1130601100 · DOI
  8. Carrell, 1998, Conformational changes and disease--serpins, prions and Alzheimer’s, Current Opinion in Structural Biology, 8, 799, 10.1016/s0959-440x(98)80101-2 · DOI
  9. Catterall, 2020, The conformational cycle of a prototypical voltage-gated sodium channel, Nature Chemical Biology, 16, 1314, 10.1038/s41589-020-0644-4 · DOI
  10. Chavez, 2015, Quantitative interactome analysis reveals a chemoresistant edgotype, Nature Communications, 6, 10.1038/ncomms8928 · DOI
  11. Chavez, 2020, Isobaric quantitative protein interaction reporter technology for comparative interactome studies, Analytical Chemistry, 92, 14094, 10.1021/acs.analchem.0c03128 · DOI
  12. Chavez, 2021, Multiplexed cross-linking with isobaric quantitative protein interaction reporter technology, Analytical Chemistry, 93, 16759, 10.1021/acs.analchem.1c02209 · DOI
  13. Chen, 2004, Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC, Cell, 119, 169, 10.1016/j.cell.2004.09.028 · DOI
  14. Chen, 2010, Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry, The EMBO Journal, 29, 717, 10.1038/emboj.2009.401 · DOI
  15. Chen, 2019, A high-speed search engine pLink 2 with systematic evaluation for proteome-scale identification of cross-linked peptides, Nature Communications, 10, 10.1038/s41467-019-11337-z · DOI
  16. Chen, 2019, Quantitative cross-linking/mass spectrometry to elucidate structural changes in proteins and their complexes, Nature Protocols, 14, 171, 10.1038/s41596-018-0089-3 · DOI
  17. Chen, 2022, Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex, Nature Structural & Molecular Biology, 29, 250, 10.1038/s41594-022-00734-6 · DOI
  18. Darling, 2018, Intrinsic disorder and posttranslational modifications: the darker side of the biological dark matter, Frontiers in Genetics, 9, 10.3389/fgene.2018.00158 · DOI
  19. Diedrich, 2013, Energy dependence of HCD on peptide fragmentation: stepped collisional energy finds the sweet spot, Journal of the American Society for Mass Spectrometry, 24, 1690, 10.1007/s13361-013-0709-7 · DOI
  20. Dion, 2003, Interactions of a DNA-bound transcriptional activator with the TBP-TFIIA-TFIIB-promoter quaternary complex, The Journal of Biological Chemistry, 278, 11495, 10.1074/jbc.M211938200 · DOI
  21. Espino, 2015, In cell footprinting coupled with mass spectrometry for the structural analysis of proteins in live cells, Analytical Chemistry, 87, 7971, 10.1021/acs.analchem.5b01888 · DOI
  22. Glossop, 2004, A conformational change in TFIIB is required for activator-mediated assembly of the preinitiation complex, Nucleic Acids Research, 32, 1829, 10.1093/nar/gkh504 · DOI
  23. Gnatt, 2001, Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution, Science, 292, 1876, 10.1126/science.1059495 · DOI
  24. Hada, 2019, Histone octamer structure is altered early in ISW2 ATP-dependent nucleosome remodeling, Cell Reports, 28, 282, 10.1016/j.celrep.2019.05.106 · DOI
  25. Hambly, 2005, Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale, Journal of the American Society for Mass Spectrometry, 16, 2057, 10.1016/j.jasms.2005.09.008 · DOI
  26. Haymond, 2019, Protein painting, an optimized MS-based technique, reveals functionally relevant interfaces of the PD-1/PD-L1 complex and the YAP2/ZO-1 complex, The Journal of Biological Chemistry, 294, 11180, 10.1074/jbc.RA118.007310 · DOI
  27. He, 2015, Extracting accurate precursor information for tandem mass spectra by rawconverter, Analytical Chemistry, 87, 11361, 10.1021/acs.analchem.5b02721 · DOI
  28. Huang, 2015, Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis, Biophysical Journal, 108, 107, 10.1016/j.bpj.2014.11.013 · DOI
  29. Ihling, 2020, The isotope-labeled, MS-cleavable cross-linker disuccinimidyl dibutyric urea for improved cross-linking/mass spectrometry studies, Journal of the American Society for Mass Spectrometry, 31, 183, 10.1021/jasms.9b00008 · DOI
  30. Kahsai, 2011, Multiple ligand-specific conformations of the β2-adrenergic receptor, Nature Chemical Biology, 7, 692, 10.1038/nchembio.634 · DOI
  31. Kays, 2000, Virtually unidirectional binding of TBP to the AdMLP TATA box within the quaternary complex with TFIIA and TFIIB, Chemistry & Biology, 7, 601, 10.1016/s1074-5521(00)00009-0 · DOI
  32. Khan, 2009, An overview of the importance of conformational flexibility in gene regulation by the transcription factors, Journal of Biophysics, 2009, 10.1155/2009/210485 · DOI
  33. Lee, 1992, TFIIA induces conformational changes in TFIID via interactions with the basic repeat, Molecular and Cellular Biology, 12, 5189, 10.1128/mcb.12.11.5189-5196.1992 · DOI
  34. Leitner, 2014, Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes, PNAS, 111, 9455, 10.1073/pnas.1320298111 · DOI
  35. Liu, 2014, Mass spectrometry footprinting reveals the structural rearrangements of cyanobacterial orange carotenoid protein upon light activation, Biochimica et Biophysica Acta - Bioenergetics, 1837, 1955, 10.1016/j.bbabio.2014.09.004 · DOI
  36. Liu, 2020, Mass spectrometry-based protein footprinting for higher-order structure analysis: fundamentals and applications, Chemical Reviews, 120, 4355, 10.1021/acs.chemrev.9b00815 · DOI
  37. Luchini, 2014, Protein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces, Nature Communications, 5, 10.1038/ncomms5413 · DOI
  38. MacLean, 2010, Skyline: an open source document editor for creating and analyzing targeted proteomics experiments, Bioinformatics, 26, 966, 10.1093/bioinformatics/btq054 · DOI · Paper page
  39. Makepeace, 2020, Improving identification of In-organello protein-protein interactions using an affinity-enrichable, isotopically coded, and mass spectrometry-cleavable chemical crosslinker, Molecular & Cellular Proteomics, 19, 624, 10.1074/mcp.RA119.001839 · DOI
  40. Mashtalir, 2018, Modular organization and assembly of SWI/SNF family chromatin remodeling complexes, Cell, 175, 1272, 10.1016/j.cell.2018.09.032 · DOI
  41. Mashtalir, 2020, A structural model of the endogenous human BAF complex informs disease mechanisms, Cell, 183, 802, 10.1016/j.cell.2020.09.051 · DOI
  42. McAlister, 2014, MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes, Analytical Chemistry, 86, 7150, 10.1021/ac502040v · DOI · Paper page
  43. McKenzie-Coe, 2022, Hydroxyl radical protein footprinting: a mass spectrometry-based structural method for studying the higher order structure of proteins, Chemical Reviews, 122, 7532, 10.1021/acs.chemrev.1c00432 · DOI
  44. Meister, 2013, An engineered calmodulin-based allosteric switch for Peptide biosensing, Chembiochem, 14, 1460, 10.1002/cbic.201300168 · DOI
  45. Mendes, 2019, An integrated workflow for crosslinking mass spectrometry, Molecular Systems Biology, 15, 10.15252/msb.20198994 · DOI
  46. Merkley, 2014, Distance restraints from crosslinking mass spectrometry: mining a molecular dynamics simulation database to evaluate lysine-lysine distances, Protein Science, 23, 747, 10.1002/pro.2458 · DOI
  47. Müller, 2001, Isotope-tagged cross-linking reagents: a new tool in mass spectrometric protein interaction analysis, Analytical Chemistry, 73, 1927, 10.1021/ac001379a · DOI
  48. Murakami, 2015, Structure of an RNA polymerase II preinitiation complex, PNAS, 112, 13543, 10.1073/pnas.1518255112 · DOI
  49. Nadeau, 2012, A review of methods used for identifying structural changes in A large protein complex, Methods in Molecular Biology, 796, 117, 10.1007/978-1-61779-334-9_7 · DOI
  50. Nikolov, 1995, Crystal structure of a TFIIB-TBP-TATA-element ternary complex, Nature, 377, 119, 10.1038/377119a0 · DOI
  51. Oberthuer, 2017, Double-flow focused liquid injector for efficient serial femtosecond crystallography, Scientific Reports, 7, 10.1038/srep44628 · DOI
  52. Patel, 2018, Structure of human TFIID and mechanism of TBP loading onto promoter DNA, Science, 362, 10.1126/science.aau8872 · DOI
  53. Patel, 2019, Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement, eLife, 8, 10.7554/eLife.54449 · DOI
  54. Petrotchenko, 2005, Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes, Molecular & Cellular Proteomics, 4, 1167, 10.1074/mcp.T400016-MCP200 · DOI
  55. Pilla, 2015, Capturing conformational States in proteins using sparse paramagnetic NMR data, PLOS ONE, 10, 10.1371/journal.pone.0127053 · DOI
  56. Prabantu, 2020, Influence of disease-causing mutations on protein structural networks, Frontiers in Molecular Biosciences, 7, 10.3389/fmolb.2020.620554 · DOI
  57. Ranish, 1991, The yeast general transcription factor TFIIA is composed of two polypeptide subunits, The Journal of Biological Chemistry, 266, 19320, 10.1016/S0021-9258(18)55000-6 · DOI
  58. Riffle, 2016, ProXL (protein cross-linking database): a platform for analysis, visualization, and sharing of protein cross-linking mass spectrometry data, Journal of Proteome Research, 15, 2863, 10.1021/acs.jproteome.6b00274 · DOI
  59. Rinas, 2016, Development of a microflow system for in-cell footprinting coupled with mass spectrometry, Analytical Chemistry, 88, 10052, 10.1021/acs.analchem.6b02357 · DOI
  60. Ruwolt, 2022, Optimized TMT-based quantitative cross-linking mass spectrometry strategy for large-scale interactomic studies, Analytical Chemistry, 94, 5265, 10.1021/acs.analchem.1c04812 · DOI
  61. Sala, 2022, Modeling of protein conformational changes with Rosetta guided by limited experimental data, Structure, 30, 1157, 10.1016/j.str.2022.04.013 · DOI · Paper page
  62. Sannigrahi, 2020, The bright and dark sides of protein conformational switches and the unifying forces of infections, Communications Biology, 3, 10.1038/s42003-020-1115-x · DOI
  63. Sengupta, 2019, Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein, eLife, 8, 10.7554/eLife.44698 · DOI
  64. Sicoli, 2019, Conformational tuning of a DNA-bound transcription factor, Nucleic Acids Research, 47, 5429, 10.1093/nar/gkz291 · DOI
  65. Tan, 1996, Crystal structure of a yeast TFIIA/TBP/DNA complex, Nature, 381, 127, 10.1038/381127a0 · DOI
  66. Telmer, 2003, Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants, The Journal of Biological Chemistry, 278, 34555, 10.1074/jbc.M301004200 · DOI
  67. Thompson, 2003, Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS, Analytical Chemistry, 75, 1895, 10.1021/ac0262560 · DOI
  68. Tsai, 2000, Structural basis of preinitiation complex assembly on human pol II promoters, The EMBO Journal, 19, 25, 10.1093/emboj/19.1.25 · DOI
  69. Tsirigotaki, 2017, Dynamics and ligand-induced conformational changes in human prolyl oligopeptidase analyzed by hydrogen/deuterium exchange mass spectrometry, Scientific Reports, 7, 10.1038/s41598-017-02550-1 · DOI
  70. Valot, 2011, MassChroQ: a versatile tool for mass spectrometry quantification, Proteomics, 11, 3572, 10.1002/pmic.201100120 · DOI
  71. Vos, 2018, Structure of activated transcription complex Pol II-DSIF-PAF-SPT6, Nature, 560, 607, 10.1038/s41586-018-0440-4 · DOI · Paper page
  72. Walzthoeni, 2015, xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry, Nature Methods, 12, 1185, 10.1038/nmeth.3631 · DOI
  73. Wang, 2017, Protein footprinting comes of age: mass spectrometry for biophysical structure assessment, Molecular & Cellular Proteomics, 16, 706, 10.1074/mcp.O116.064386 · DOI
  74. Wippel, 2022, Quantitative interactome analysis with chemical cross-linking and mass spectrometry, Current Opinion in Chemical Biology, 66, 10.1016/j.cbpa.2021.06.011 · DOI
  75. Yu, 2016, Developing a multiplexed quantitative cross-linking mass spectrometry platform for comparative structural analysis of protein complexes, Analytical Chemistry, 88, 10301, 10.1021/acs.analchem.6b03148 · DOI
  76. Zheng, 2019, Protein dynamics and conformational changes explored by hydrogen/deuterium exchange mass spectrometry, Current Opinion in Structural Biology, 58, 305, 10.1016/j.sbi.2019.06.007 · DOI
  77. Zhou, 2013, Covalent labeling with isotopically encoded reagents for faster structural analysis of proteins by mass spectrometry, Analytical Chemistry, 85, 9664, 10.1021/ac401978w · DOI

Metadata

Authors
Luo, J., & Ranish, J.
Affiliations
  • Institute for Systems Biology (US)
  • Institute for Systems Biology
Venue
eLife
Published
2024-11-14
Volume
13
ISSN
2050-084X (ISSN-L)
OpenAlex
W4404376995
Cited by
2
References
3
Citations by year
2025: 2
FWCI
0.25
Type
journal article
Language
en
Open access
Locations
  • eLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
Funders
National Institutes of Health (RO1GM136974, RO1GM108908, R01GM144559)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
protein conformational change, protein complexes, transcription factor complex, TATA-binding protein, TFIIA, TFIIB, RNA polymerase II, biosensors, ternary complex

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. https://app.cochat.ai/papers/10.7554/elife.99809.3
The paper
Luo, J., & Ranish, J. (2024). Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. eLife. https://doi.org/10.7554/elife.99809.3