Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay.
FtsA, a member of the ATPase superfamily that includes actin and bacterial actin homologs, is essential for cell division of Escherichia coli and is recruited to the Z ring. In turn, recruitment of later essential division proteins to the Z ring is dependent on FtsA. In a polar recruitment assay, we found that FtsA can recruit at least two late proteins, FtsI and FtsN, to the cell poles independently of Z rings. Moreover, a unique structural domain of FtsA, subdomain 1c, which is divergent in the other ATPase superfamily members, is sufficient for this recruitment but not required for the ability of FtsA to localize to Z rings. Surprisingly, targeting the 1c subdomain to the Z ring by fusing it to FtsZ could partially suppress a thermosensitive ftsA mutation. These results suggest that subdomain 1c of FtsA is a completely independent functional domain with an important role in interacting with a septation protein subassembly.
Corbin
Brian D
BD
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030, USA.
Geissler
Brett
B
Sadasivam
Mahalakshmi
M
Margolin
William
W
D002455:Cell Division; D016764:Cell Polarity; D003470:Culture Media; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D046915:Penicillin-Binding Proteins / Q000378:metabolism*; D046928:Peptidoglycan Glycosyltransferase / Q000378:metabolism*; D016335:Zinc Fingers
D003470:Culture Media; D029968:Escherichia coli Proteins; C489310:FtsA protein, E coli; C478704:FtsI protein, E coli; C098711:FtsN protein, E coli; C076835:FtsZ84 protein, E coli; D008565:Membrane Proteins; D046915:Penicillin-Binding Proteins; D046928:Peptidoglycan Glycosyltransferase