The Transmembrane Helix of the Escherichia coli Division Protein FtsI Localizes to the Septal Ring
| Autor: | Jennifer L. Wendt, Mark C. Wissel, David S. Weiss, Calista J. Mitchell |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Cytoplasm
Peptidoglycan glycosyltransferase Escherichia coli Proteins Molecular Sequence Data Periplasmic space Biology Microbiology Protein Structure Secondary Green fluorescent protein Cell biology Microbial Cell Biology Transmembrane domain A-site chemistry.chemical_compound Biochemistry chemistry Periplasm Penicillin-Binding Proteins Amino Acid Sequence Peptidoglycan Glycosyltransferase Peptidoglycan Erratum Molecular Biology Peptide sequence |
| Zdroj: | Journal of Bacteriology. 187:320-328 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.187.1.320-328.2005 |
| Popis: | FtsI (also called PBP3) of Escherichia coli is a transpeptidase required for synthesis of peptidoglycan in the division septum and is one of about a dozen division proteins that localize to the septal ring. FtsI comprises a short amino-terminal cytoplasmic domain, a single transmembrane helix (TMH), and a large periplasmic domain that encodes the catalytic (transpeptidase) activity. We show here that a 26-amino-acid fragment of FtsI is sufficient to direct green fluorescent protein to the septal ring in cells depleted of wild-type FtsI. This fragment extends from W22 to V47 and corresponds to the TMH. This is a remarkable finding because it is usual for a TMH to target a protein to a site more specific than the membrane. Alanine-scanning mutagenesis of the TMH identified several residues important for septal localization. These residues cluster on one side of an alpha-helix, which we propose interacts directly with another division protein to recruit FtsI to the septal ring. |
| Databáze: | OpenAIRE |
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