STPKINTB

Protein kinases in metabolic regulation in Mycobacterium tuberculosis

 Coordinatore UNIVERSITY OF LEICESTER 

 Organization address address: University Road
city: LEICESTER
postcode: LE1 7RH

contact info
Titolo: Ms.
Nome: Marie
Cognome: Adams
Email: send email
Telefono: +44 116 223 1799
Fax: +44 116 252 2028

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 45˙000 €
 EC contributo 45˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-ERG-2008
 Funding Scheme MC-ERG
 Anno di inizio 2008
 Periodo (anno-mese-giorno) 2008-11-01   -   2012-04-29

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    UNIVERSITY OF LEICESTER

 Organization address address: University Road
city: LEICESTER
postcode: LE1 7RH

contact info
Titolo: Ms.
Nome: Marie
Cognome: Adams
Email: send email
Telefono: +44 116 223 1799
Fax: +44 116 252 2028

UK (LEICESTER) coordinator 45˙000.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

nitrogen    regulatory    kinase    regulation    metabolism    protein    virulence    pkng    pknb   

 Obiettivo del progetto (Objective)

'The genome of Mycobacterium tuberculosis contains 11 serine threonine protein kinases. Amongst these PknA, PknB and PknG are essential for bacterial survival and/or virulence, and are considered potential drug targets. This proposal aims to elucidate the functions of PknB and PknG, with particular focus on the regulation of primary metabolism. PknB is reported to be involved in the control of cell-shape, whereas PknG might function as a regulator of metabolism or as a virulence protein secreted into the macrophage. Based on a study of the related microbe Corynebacterium glutamicum, preliminary work has been done to investigate a possible role for PknG (and possibly PknB) in regulation of the citric acid cycle. In corynebacteria PknG controls the phosphorylation status of a small regulatory protein GarA, which directly inhibits the ODH complex. First experiments with mycobacteria suggest that this regulatory mechanism is probably conserved and may also be employed to regulate nitrogen metabolism in these organisms. An experimental strategy is proposed to investigate the regulation of kinase activity and determine the effects of kinase activity on carbon and nitrogen metabolism.'

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