PGRECONST

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

 Coordinatore 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

 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

Mappa


 Word cloud

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

proteins    synthesis    cycle    septosome    complexes    host    elongasome    lab    cell    pg    protein    interactions    environment   

 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.'

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