PGRECONST

Assembly and coordination of peptidoglycan synthesis complexes during bacterial growth and cell division

Coordinatore	UNIVERSITY OF NEWCASTLE UPON TYNE    more  Organization address address: Kensington Terrace 6 city: NEWCASTLE UPON TYNE postcode: NE1 7RU contact info Titolo: Mrs. Nome: Donna Cognome: Armstrong Email: send email Telefono: +44 1912824525 Fax: +44 1912824524
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	221˙606 €
EC contributo	221˙606 €
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-2013-IEF
Funding Scheme	MC-IEF
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-04-01   -   2016-03-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	UNIVERSITY OF NEWCASTLE UPON TYNE  Organization address address: Kensington Terrace 6 city: NEWCASTLE UPON TYNE postcode: NE1 7RU contact info Titolo: Mrs. Nome: Donna Cognome: Armstrong Email: send email Telefono: +44 1912824525 Fax: +44 1912824524	UK (NEWCASTLE UPON TYNE)	coordinator	221˙606.40

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 Obiettivo del progetto (Objective)

'In this project, I will investigate the proteins involved, and their interactions, in the formation of both peptidoglycan (PG) synthesis core complexes (elongasome and septosome) in the model bacterium Escherichia coli to gain new molecular insights into how the cell grows its cell wall during the cell cycle. This will be achieved by: (i) in vivo characterization of new or already known important interactions within or between the PG synthesis machineries. This part of the project will provide relevant information about the hierarchy or requirement between the proteins involved in the process, which is essential information for the following more detailed mechanistic studies; (ii) studying the PG protein interactions and enzymatic activities during the intermediate step between the elongation and the cell division processes, which will provide new insight in how elongasome and septosome complexes are connected and regulated during the cell cycle, one of the most important unknown processes in the research area; and (iii) reconstructing the elongasome and septosome activities in a more natural environment to quantify the activities and study the properties of each protein involved. During the proposed project, I will obtain knowledge and skills in purification and handling of membrane proteins, in vitro reconstitution approaches and cutting-edge techniques available in the host lab and institute. The top-ranked host lab and collaborators will provide me the best environment for my scientific development, enhancing my competences in the field.'