Localization of FtsL to the Escherichia coli septal ring
In Escherichia coli, nine gene products are known to be essential for assembly of the division septum. One of these, FtsL, is a bitopic membrane protein whose precise function is not understood. Here we use fluorescence microscopy to study the subcellular localization of FtsL, both in a wild‐type st...
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| Veröffentlicht in: | Molecular microbiology 1999-01, Vol.31 (2), p.725-737 |
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| creator | Ghigo, Jean‐Marc Weiss, David S. Chen, Joseph C. Yarrow, Justin C. Beckwith, Jon |
| description | In Escherichia coli, nine gene products are known to be essential for assembly of the division septum. One of these, FtsL, is a bitopic membrane protein whose precise function is not understood. Here we use fluorescence microscopy to study the subcellular localization of FtsL, both in a wild‐type strain and in a merodiploid strain that expresses a GFP–FtsL fusion protein. We show that FtsL localizes to the cell septum where it forms a ring analogous to the cytoplasmic FtsZ ring. FtsL localization is dependent upon the function of FtsZ, FtsA and FtsQ, but not FtsI. In a reverse approach, we use fusions of green fluorescent protein (GFP) to FtsZ, FtsA and ZipA to show that these proteins localize to the division site in an FtsL‐independent fashion. We propose that FtsL is a relatively late recruit to the ring structure that mediates septation. |
| doi_str_mv | 10.1046/j.1365-2958.1999.01213.x |
| format | Article |
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One of these, FtsL, is a bitopic membrane protein whose precise function is not understood. Here we use fluorescence microscopy to study the subcellular localization of FtsL, both in a wild‐type strain and in a merodiploid strain that expresses a GFP–FtsL fusion protein. We show that FtsL localizes to the cell septum where it forms a ring analogous to the cytoplasmic FtsZ ring. FtsL localization is dependent upon the function of FtsZ, FtsA and FtsQ, but not FtsI. In a reverse approach, we use fusions of green fluorescent protein (GFP) to FtsZ, FtsA and ZipA to show that these proteins localize to the division site in an FtsL‐independent fashion. 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One of these, FtsL, is a bitopic membrane protein whose precise function is not understood. Here we use fluorescence microscopy to study the subcellular localization of FtsL, both in a wild‐type strain and in a merodiploid strain that expresses a GFP–FtsL fusion protein. We show that FtsL localizes to the cell septum where it forms a ring analogous to the cytoplasmic FtsZ ring. FtsL localization is dependent upon the function of FtsZ, FtsA and FtsQ, but not FtsI. In a reverse approach, we use fusions of green fluorescent protein (GFP) to FtsZ, FtsA and ZipA to show that these proteins localize to the division site in an FtsL‐independent fashion. 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| source | MEDLINE; Wiley Journals; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Free Full-Text Journals in Chemistry |
| subjects | Bacterial Proteins - genetics Bacterial Proteins - metabolism Carrier Proteins - genetics Carrier Proteins - metabolism Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Cytoskeletal Proteins Escherichia coli Escherichia coli - growth & development Escherichia coli - metabolism Escherichia coli Proteins Green Fluorescent Proteins Hexosyltransferases - genetics Hexosyltransferases - metabolism Luminescent Proteins - genetics Luminescent Proteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Microscopy, Fluorescence Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Muramoylpentapeptide Carboxypeptidase Penicillin-Binding Proteins Peptidoglycan Glycosyltransferase Peptidyl Transferases - genetics Peptidyl Transferases - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism |
| title | Localization of FtsL to the Escherichia coli septal ring |
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