Functional analysis of the cell division protein FtsW of Escherichia coli
| Autor: | Robert Brasseur, Tanneke den Blaauwen, Claudine Fraipont, Martine Nguyen-Distèche, Soumya Pastoret, Benoît Wolf, Mirjam E. G. Aarsman, Annick Thomas, André Piette |
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| Přispěvatelé: | Molecular Cytology (SILS, FNWI) |
| Rok vydání: | 2004 |
| Předmět: |
Cell division
Recombinant Fusion Proteins Green Fluorescent Proteins Peptide Peptidoglycan Biology medicine.disease_cause Microbiology Microbial Cell Biology chemistry.chemical_compound Bacterial Proteins medicine Escherichia coli Image Processing Computer-Assisted Molecular Biology chemistry.chemical_classification Genetic Complementation Test Membrane Proteins Periplasmic space Transmembrane protein Amino acid chemistry Membrane protein Biochemistry Microscopy Fluorescence Mutagenesis Site-Directed Cell Division |
| Zdroj: | Journal of Bacteriology, 186, 8370-8379. American Society for Microbiology |
| ISSN: | 0021-9193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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