Septation in Escherichia coli requires several gene products. One of these,
FtsQ, is a simple bitopic membrane protein with a short cytoplasmic N term
inus, a membrane-spanning segment, and a periplasmic domain. We have constr
ucted a merodiploid strain that expresses both FtsQ and the fusion protein
green fluorescent protein (GFP)-FtsQ from single-copy chromosomal genes. Th
e gfp-ftsQ gene complements a null mutation in pse Fluorescence microscopy
revealed that GFP-FtsQ localizes to the division site. Replacing the cytopl
asmic and transmembrane domains of FtsQ with alternative membrane anchors d
id not prevent the localization of the GFP fusion protein, while replacing
the periplasmic domain did, suggesting that the periplasmic domain is neces
sary and sufficient for septal targeting. GFP-FtsQ localization to the sept
um depended on the cell division proteins FtsZ and FtsA, which are cytoplas
mic, but not on FtsL and FtsI, which are bitopic membrane proteins with com
paratively large periplasmic domains. In addition, the septal localization
of ZipA apparently did not require functional FtsQ. Our results indicate th
at FtsQ is an intermediate recruit to the division site.