The UvA-LINKER will give you a range of other options to find the full text of a publication (including a direct link to the full-text if it is located on another database on the internet).
De UvA-LINKER biedt mogelijkheden om een publicatie elders te vinden (inclusief een directe link naar de publicatie online als deze beschikbaar is in een database op het internet).
faculty: "FNWI" and publication year: "2004"
| Authors||S. Pastoret, C. Fraipont, T. den Blaauwen, B. Wolf, A. Thomas, R. Brasseur, M.E.G. Aarsman, A. Piette, M. Nguyen-Disteche|
|Title||Functional analysis of the cell division protein FtsW of Escherichia coli.|
|Journal||Journal of Bacteriology|
|Faculty||Faculty of Science|
|Institute/dept.||FNWI: Swammerdam Institute for Life Sciences (SILS)|
|Keywords||Membrane Proteins; Cell Division; Fluorescence Microscopy; Site-directed mutagenesis; Peptidoglycan|
|Classification||35.75 ; 42.15 |
|Abstract||Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation. This essential cell division protein has 10 transmembrane segments (TMSs). It is a late recruit to the division site and is required for subsequent recruitment of penicillin-binding protein 3 (PBP3) catalyzing peptide cross-linking. The results allow identification of several domains of the protein with distinct functions. The localization of PBP3 to the septum was found to be dependent on the periplasmic loop located between TMSs 9 and 10. The E240-A249 amphiphilic peptide in the periplasmic loop between TMSs 7 and 8 appears to be a key element in the functioning of FtsW in the septal peptidoglycan assembly machineries. The intracellular loop (containing the R166-F178 amphiphilic peptide) between TMSs 4 and 5 and Gly 311 in TMS 8 are important components of the amino acid sequence-folding information.|
Use this url to link to this page: http://dare.uva.nl/en/record/148802
Contact us about this recordNotify a colleague
Add to bookbag