Advanced search
1 file | 1.39 MB Add to list

ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry

Yurong Wen (UGent) , Frank Sobott and Bart Devreese (UGent)
Author
Organization
Abstract
Toxin-antitoxin systems are genetic modules involved in a broad range of bacterial cellular processes including persistence, multidrug resistance and tolerance, biofilm formation, and pathogenesis. In type II toxin-antitoxin systems, both the toxin and antitoxin are proteins. In the prototypic Escherichia coli HipA-HipB module, the antitoxin HipB forms a complex with the protein kinase HipA and sequesters it in the nucleoid. HipA is then no longer able to phosphorylate glutamyl-tRNA-synthetase and this prevents the initiation of the forthcoming stringent response. Here we investigated the assembly of the Shewanella oneidensis MR-1 HipA-HipB complex using native electrospray ion mobility-mass spectrometry and chemical crosslinking combined with mass spectrometry. We revealed that the HipA autophosphorylation was accompanied by a large conformational change, and confirmed structural evidence that S. oneidensis MR-1 HipA-HipB assembly was distinct from the prototypic E. coli HipA-HipB complex.
Keywords
Ion mobility, Chemical crosslinking, HipAB, Toxin-antitoxin system, Mass spectrometry, SHEWANELLA-ONEIDENSIS MR-1, TOXIN-ANTITOXIN SYSTEMS, MULTIDRUG TOLERANCE, BACTERIAL NANOWIRES, BIOFILM FORMATION, LINKED PEPTIDES, DRUG DISCOVERY, PERSISTENCE, COMPLEXES, BIOLOGY

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 1.39 MB

Citation

Please use this url to cite or link to this publication:

MLA
Wen, Yurong, Frank Sobott, and Bart Devreese. “ATP and Autophosphorylation Driven Conformational Changes of HipA Kinase Revealed by Ion Mobility and Crosslinking Mass Spectrometry.” ANALYTICAL AND BIOANALYTICAL CHEMISTRY 408.21 (2016): 5925–5933. Print.
APA
Wen, Y., Sobott, F., & Devreese, B. (2016). ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry. ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 408(21), 5925–5933.
Chicago author-date
Wen, Yurong, Frank Sobott, and Bart Devreese. 2016. “ATP and Autophosphorylation Driven Conformational Changes of HipA Kinase Revealed by Ion Mobility and Crosslinking Mass Spectrometry.” Analytical and Bioanalytical Chemistry 408 (21): 5925–5933.
Chicago author-date (all authors)
Wen, Yurong, Frank Sobott, and Bart Devreese. 2016. “ATP and Autophosphorylation Driven Conformational Changes of HipA Kinase Revealed by Ion Mobility and Crosslinking Mass Spectrometry.” Analytical and Bioanalytical Chemistry 408 (21): 5925–5933.
Vancouver
1.
Wen Y, Sobott F, Devreese B. ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry. ANALYTICAL AND BIOANALYTICAL CHEMISTRY. 2016;408(21):5925–33.
IEEE
[1]
Y. Wen, F. Sobott, and B. Devreese, “ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry,” ANALYTICAL AND BIOANALYTICAL CHEMISTRY, vol. 408, no. 21, pp. 5925–5933, 2016.
@article{8150308,
  abstract     = {Toxin-antitoxin systems are genetic modules involved in a broad range of bacterial cellular processes including persistence, multidrug resistance and tolerance, biofilm formation, and pathogenesis. In type II toxin-antitoxin systems, both the toxin and antitoxin are proteins. In the prototypic Escherichia coli HipA-HipB module, the antitoxin HipB forms a complex with the protein kinase HipA and sequesters it in the nucleoid. HipA is then no longer able to phosphorylate glutamyl-tRNA-synthetase and this prevents the initiation of the forthcoming stringent response. Here we investigated the assembly of the Shewanella oneidensis MR-1 HipA-HipB complex using native electrospray ion mobility-mass spectrometry and chemical crosslinking combined with mass spectrometry. We revealed that the HipA autophosphorylation was accompanied by a large conformational change, and confirmed structural evidence that S. oneidensis MR-1 HipA-HipB assembly was distinct from the prototypic E. coli HipA-HipB complex.},
  author       = {Wen, Yurong and Sobott, Frank and Devreese, Bart},
  issn         = {1618-2642},
  journal      = {ANALYTICAL AND BIOANALYTICAL CHEMISTRY},
  keywords     = {Ion mobility,Chemical crosslinking,HipAB,Toxin-antitoxin system,Mass spectrometry,SHEWANELLA-ONEIDENSIS MR-1,TOXIN-ANTITOXIN SYSTEMS,MULTIDRUG TOLERANCE,BACTERIAL NANOWIRES,BIOFILM FORMATION,LINKED PEPTIDES,DRUG DISCOVERY,PERSISTENCE,COMPLEXES,BIOLOGY},
  language     = {eng},
  number       = {21},
  pages        = {5925--5933},
  title        = {ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry},
  url          = {http://dx.doi.org/10.1007/s00216-016-9709-3},
  volume       = {408},
  year         = {2016},
}

Altmetric
View in Altmetric
Web of Science
Times cited: