Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Oligomeric states in sodium ion–dependent regulation of cyanobacterial histidine kinase-2

View ORCID ProfileIskander M. Ibrahim, Liang Wang, Sujith Puthiyaveetil, Norbert Krauß, View ORCID ProfileJon Nield, View ORCID ProfileJohn F. Allen
doi: https://doi.org/10.1101/140145
Iskander M. Ibrahim
aSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK
bDepartment of Biochemistry, Purdue University, Indiana, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Iskander M. Ibrahim
Liang Wang
aSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Sujith Puthiyaveetil
aSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK
bDepartment of Biochemistry, Purdue University, Indiana, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Norbert Krauß
cBotanisches Institut, Karlsruher Institut für Technologie, Karlsruhe, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Jon Nield
aSchool of Biological and Chemical Sciences, Queen Mary University of London, London, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Jon Nield
John F. Allen
dResearch Department of Genetics, Evolution and Environment, University College London, London, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for John F. Allen
  • For correspondence: j.f.allen@ucl.ac.uk
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

ABSTRACT

Two-component signal transduction systems (TCSs) consist of sensor histidine kinases and response regulators. TCSs mediate adaptation to environmental changes in bacteria, plants, fungi, and protists. Histidine kinase 2 (Hik2) is a sensor histidine kinase found in all known cyanobacteria and as chloroplast sensor kinase in eukaryotic algae and plants. Sodium ions have been shown to inhibit the autophosphorylation activity of Hik2 that precedes phosphoryl transfer to response regulators, but the mechanism of inhibition has not been determined. We report on the mechanism of Hik2 activation and inactivation probed by chemical crosslinking and size exclusion chromatography together with direct visualisation of the kinase using negative-stain transmission electron microscopy of single particles. We show that the functional form of Hik2 is a higher order oligomer such as a hexamer or octamer. Increased NaCl concentration converts the active hexamer into an inactive tetramer. Furthermore, the action of NaCl appears to be confined to the Hik2 kinase domain.

IMPORTANCE Bacteria sense change and respond to it by means of two-component regulatory systems. The sensor component is a protein that becomes covalently modified by a phosphate group on a histidine side chain. The response regulator accepts the phosphate group onto an aspartate, with structural and functional consequences, often for gene transcription. Histidine kinase 2 is a sensor of sodium ion concentration and redox potential, regulating transcription of genes for light-harvesting and reaction center proteins of photosynthesis in cyanobacteria and chloroplasts of algae and plants. Using radiolabeling, chemical crosslinking, chromatography and electron microscopy, we find that sodium ion concentration governs the oligomeric state of Histidine Kinase 2 and its phosphorylation by ATP.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
Back to top
PreviousNext
Posted May 19, 2017.
Download PDF
Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Oligomeric states in sodium ion–dependent regulation of cyanobacterial histidine kinase-2
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Oligomeric states in sodium ion–dependent regulation of cyanobacterial histidine kinase-2
Iskander M. Ibrahim, Liang Wang, Sujith Puthiyaveetil, Norbert Krauß, Jon Nield, John F. Allen
bioRxiv 140145; doi: https://doi.org/10.1101/140145
Reddit logo Twitter logo Facebook logo LinkedIn logo Mendeley logo
Citation Tools
Oligomeric states in sodium ion–dependent regulation of cyanobacterial histidine kinase-2
Iskander M. Ibrahim, Liang Wang, Sujith Puthiyaveetil, Norbert Krauß, Jon Nield, John F. Allen
bioRxiv 140145; doi: https://doi.org/10.1101/140145

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Biochemistry
Subject Areas
All Articles
  • Animal Behavior and Cognition (4237)
  • Biochemistry (9155)
  • Bioengineering (6797)
  • Bioinformatics (24052)
  • Biophysics (12149)
  • Cancer Biology (9562)
  • Cell Biology (13814)
  • Clinical Trials (138)
  • Developmental Biology (7653)
  • Ecology (11729)
  • Epidemiology (2066)
  • Evolutionary Biology (15534)
  • Genetics (10663)
  • Genomics (14346)
  • Immunology (9503)
  • Microbiology (22876)
  • Molecular Biology (9113)
  • Neuroscience (49080)
  • Paleontology (357)
  • Pathology (1487)
  • Pharmacology and Toxicology (2576)
  • Physiology (3851)
  • Plant Biology (8347)
  • Scientific Communication and Education (1473)
  • Synthetic Biology (2299)
  • Systems Biology (6202)
  • Zoology (1302)