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Morphogenesis of rod-shaped sacculi

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dc.contributor European Commission
dc.contributor Netherlands Organization for Scientific Research
dc.contributor Ministerio de Educación y Ciencia (España)
dc.contributor Fundación Ramón Areces
dc.creator Blaauwen, Tanneke den
dc.creator Pedro, Miguel Ángel de
dc.creator Nguyen-Distèche, Martine
dc.creator Ayala, Juan Alfonso
dc.date 2008-05-23T12:16:26Z
dc.date 2008-05-23T12:16:26Z
dc.date 2008-02
dc.date.accessioned 2017-01-31T01:26:55Z
dc.date.available 2017-01-31T01:26:55Z
dc.identifier FEMS Microbiol Rev. 2008 Mar;32(2):321-44. Review
dc.identifier 0168-6445
dc.identifier http://hdl.handle.net/10261/4508
dc.identifier 10.1111/j.1574-6976.2007.00090.x
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/4508
dc.description The definitive version is available at www.blackwell-synergy.com http://dx.doi.org/10.1111/j.1574-6976.2007.00098.x
dc.description For growth and division of rod-shaped bacteria, the cylindrical part of the sacculus has to be elongated and two new cell poles have to be synthesized. The elongation is performed by a protein complex, the elongase that inserts disaccharidepentapeptide units at a limited number of discrete sites while using the cytoskeletal MreB helix as a tracking device. Upon initiation of cell division by positioning of the cytoskeletal Z-ring at mid cell, a switch from dispersed to concentrated local peptidoglycan-synthesis occurs. From this point on, peptidoglycan synthesis is for a large part redirected from elongating activity to synthesis of new cell poles by the divisome. The divisome might be envisioned as an extended elongase because apart from its basic peptidoglycan synthesizing activity, specific functions have to be added. These are conversion from a cylinder to a sphere, invagination of the outer membrane and addition of hydrolases that allow separation of the daughter cells. The elongase and the divisome are dynamic hyperstructures that probably share part of their proteins. Although this multifunctionality and flexibility form a barrier to the functional elucidation of its individual subunits, it helps the cells to survive a variety of emergency situations and to proliferate securely.
dc.description This work was supported in part by the European commission within the ‘EUR-INTAFAR’ LSHM-CT-2004-512138, and ‘COBRA’ LSHM-CT-2003-503335 networks and by a Vernieuwingsimpuls grant 016.001.024 of the Netherlands Organization for Scientific Research (NWO)to T.d.B., by the Belgian State, Prime Minister’s Office, Science Policy programming (IAP no. P6/19), the Actions de Recherche Concert´ees (grant no. 03/08-297), the Fond de la Recherche Fondamentale Collective (contract no. 2.4543.05) to M.N., and BFU2006-04574 from Ministerio de Educación y Ciencia, Spain, to J.A.A. and an institutional grant from Fundación Ramón Areces.
dc.description Peer reviewed
dc.format 22195 bytes
dc.format application/pdf
dc.language eng
dc.publisher Blackwell Publishing
dc.rights openAccess
dc.subject Cell division
dc.subject Divisome
dc.subject Elongase
dc.subject Escherichia coli
dc.subject PBP
dc.subject Peptidoglycan
dc.title Morphogenesis of rod-shaped sacculi
dc.type Artículo


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