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Bacilliredoxins and bacillithiol: Unique redox systems amongst the Bacilli (DTP 025 U13)

Information

  • Start date: October 2013
  • Programme: PhD
  • Mode of Study: Full Time
  • Studentship Length: 4 years

How to Apply

Fees & Funding

  • Funding Status: Competition Funded Project (EU Students Only)
    Further Details
  • Funding Conditions:

    Funding for PhD studentships from BBSRC is available to successful candidates who meet the UK Research Council eligibility criteria including the 3-year residency requirements in the UK.  These requirements are detailed in the BBSRC eligibility guide which can be found below. In most cases UK and EU nationals who have been ordinarily resident in the UK for 3 years prior to the start of the course are eligible for a full-award.  Other EU nationals may qualify for a fees only award. Below is the link to the BBSRC PhD studentship eligibility guidelines which all candidates should check to confirm their eligibility for funding.

    http://www.bbsrc.ac.uk/web/FILES/Guidelines/studentship_eligibility.pdf  The current stipend for 2012/13 is £13,590 per annum.

  • Fees: Fees Information (Opens in new window)

Entry Requirements

  • Acceptable First Degree:

    A first or upper second class UK honours degree, or the equivalent qualifications gained outside the UK, in an appropriate area of science or technology.

Project Description

Glutathione (GSH) is the predominant thiol redox buffer in Eukaryotes and Gram negative bacteria. Protein glutathionylation (formation of GSS-protein mixed disulfides) is employed in the redox regulation of protein function and to protect exposed cysteine residues from irreversible damage during oxidative stress. The reversibility of protein glutathionylation is mediated by glutaredoxin (Grx) enzymes, which reductively regenerate the free protein thiols.[1] Gram positive bacteria do not produce GSH.

Bacillithiol (BSH) has been identified as the GSH surrogate amongst many Bacilli and low G+C Gram positive bacteria (ie Firmicutes).[2] These include several bacteria of medical, commercial and environmental importance such as Staphylococcus aureus and Bacillus anthracis (microbial pathogens), Bacillus subtilis and Bacillus cereus (food spoilage). Protein-S-bacillithiolation was recently identified in B. subtilis as a defence mechanism in response to oxidative stress.[3] Three candidate bacilliredoxins (Brx) and a bacillithiol disulfide reductase have been identified that are conserved amongst other BSH-producing bacteria.

We will unravel the unique characteristics of this newly discovered redox system to address these fundamental questions about BSH redox biology using Bacillus subtilis as a model microorganism. The fundamental BSH/Brx redox pathways revealed in B. subtilis willlikely be mirrored in other BSH-utilising bacteria of medical, agricultural and environmental importance.

This project offers a strong platform of interdisciplinary research training in aspects of protein biochemistry, enzymology, molecular biology and redox proteomics. There are also opportunities to visit the lab of Dr Graham Christie (University of Cambridge) to be trained in redox-sensitive green fluorescence protein methodologies.

In keeping with the postgraduate training policy of the Biotechnology and Biological Sciences Research Council (BBSRC) all students recruited onto this programme will be expected to undertake a three months internship during the second or third year of their degree. The internship will offer exciting and invaluable experience of work in an area outside of research, and full support and advice will be provided by a professional team from the UEA.

This project has been shortlisted for funding by the Norwich Biosciences Doctoral Training Partnership (DTP) – a collaboration between the Norwich Biosciences Institutes and the University of East Anglia.  For further information and application details please see the Norwich Biosciences DTP website: http://biodtp.norwichresearchpark.ac.uk/

References

Free Rad. Biol. Med. 2007, 43, 883; [2] Nat. Chem. Biol. 2009, 5, 625-627; [3] S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in Firmicutes bacteria Antiox Red. Signal. (in press).



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