| dc.contributor.author | Ibrahim, Iskander Mohamed | |
| dc.date.accessioned | 2015-09-08T11:02:16Z | |
| dc.date.available | 2015-09-08T11:02:16Z | |
| dc.date.issued | 2013-02 | |
| dc.identifier.citation | Ibrahim, I.M. 2013. Biochemical characterisation of the cyanobacterial Hik2-Rre1 two-component regulatory system. Queen Mary University of London. | en_US |
| dc.identifier.uri | http://qmro.qmul.ac.uk/xmlui/handle/123456789/8509 | |
| dc.description | PhD | en_US |
| dc.description.abstract | Two-component signal transduction systems (TCS) consist of a sensor histidine
kinase and a response regulator. TCS are ubiquitous in prokaryotes, but found
only in some eukaryotes. TCS mediate adaptation to various environmental
changes in bacteria, plants, fungi, and protists. Histidine kinase 2 (Hik2) is a
sensor histidine kinase found in all cyanobacteria. The Hik2 homologue known
as Chloroplast Sensor Kinase is found in algae and plants, where it is encoded by
the nuclear genome and it is targeted to chloroplasts. CSK couples the redox state
of the photosynthetic electron transport chain to chloroplast gene transcription.
This thesis describes biochemical characterisation of the signal transduction
mechanism of Hik2 and its response regulator (Rre) partners in order to clarify the
Hik2-Rre two-component signal transduction pathway. Results presented in this
thesis illustrate that the autophosphorylation activity of the full-length Hik2
protein is specifically inhibited by sodium ions. An autophosphorylation event of
a histidine kinase is the result of homodimerisation and is followed by trans or
cis-autophosphorylation of each monomer on its conserved histidine residue.
Chemical crosslinking revealed that the Hik2 protein exists predominantly as a
phosphorylated (autokinase active) monomer, tetramer, and higher-order
oligomeric complexes. The functions of these different oligomeric states of Hik2
are also discussed. From a previous study, which was based on an observation
from a yeast two-hybrid assay, Hik2 was proposed to form a two-component pair
with Rre1 and RppA. However, no further evidence was presented to support
either direct interaction or direct phosphotransfer activity of the Hik2-Rre pair.
This thesis confirms interaction of Hik2-Rre1 and Hik2-RppA two-component
! %!
pairs using an in vitro pull-down assay and phosphotransfer kinetics. Finally, a
model is proposed for the Hik2 based two-component signal transduction pathway. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | Queen Mary University of London | en_US |
| dc.subject | Biochemistry | en_US |
| dc.title | Biochemical characterisation of the cyanobacterial Hik2-Rre1 two-component regulatory system. | en_US |
| dc.type | Thesis | en_US |
| dc.rights.holder | The copyright of this thesis rests with the author and no quotation from it or information derived from it may be published without the prior written consent of the author | |
