Disease relevance of ECs0097

• An amino-proximal domain required for the localization of FtsQ in the cytoplasmic membrane, and for its biological function in Escherichia coli [1].
• The Bacillus subtilis cell-division protein DivIB is shown to be present at an approximately 100-fold higher abundance (approximately 5000 molecules per cell) than its Escherichia coli FtsQ homologue [2].
• Identification and characterization of the DdlB, FtsQ and FtsA genes upstream of FtsZ in Bartonella bacilliformis and Bartonella henselae [3].
• The DdlB, FtsQ, and FtsA proteins from Bartonella species are most homologous to proteins in closely related species from the Order Rhizobiales, such as Brucella sp., Agrobacterium tumefaciens, and M. loti [3].

High impact information on ECs0097

• Here we present a method--premature targeting--for bypassing the normal localization requirements of a cell division protein and apply it to FtsQ, a protein recruited midway through the pathway [4].
• FtsL and FtsB, which each contain a leucine zipper-like sequence, are dependent on each other for this localization, and each of them is dependent on FtsQ [5].
• Rather, this mutation acts as a general suppressor of division defects, which include deletions of the normally essential genes zipA and ftsK and mutations in FtsQ that affect both localization and recruitment [6].
• We used a sensitive assay involving biotinylation to show that all of the mutations caused defects in the membrane insertions of three topologically distinct membrane proteins, AcrB, MalF, and FtsQ [7].
• PBP 1B was apparently endowed with a more versatile biosynthetic potential that permitted a substantial enlargement of PBP 1A-deficient cells when PBP 2 or 3 was inhibited or when FtsQ was inactive. beta-Lactams binding to PBP 2 (mecillinam) or 3 (furazlocillin) caused rapid lysis in a ponB background [8].

Biological context of ECs0097

• The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations [9].
• Recent evidence is presented indicating that the normal rod cell shape can be abandoned, allowing growth as a coccus, either by increasing the amount of the division proteins FtsZ, FtsA and FtsQ, or by increasing the pool of the nucleotide ppGpp [10].

Anatomical context of ECs0097

• A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region [5].
• Finally, a membrane protein possessing a large periplasmic region (FtsQ) and therefore requiring both factors (SRP/SR and SecA/SecB) for membrane integration/translocation was also shown to be integrated correctly in this cell-free system [11].
• FtsQ and MraY, obviously nonfunctional in the L-form, are essential for cell division and cell wall synthesis, respectively, in all bacteria with a peptidoglycan-based cell wall [12].

Associations of ECs0097 with chemical compounds

• Division in the absence of PBP2 activity is restored (and resistance to mecillinam is conferred) when the three cell division proteins FtsQ, FtsA and FtsZ are overproduced, but not when only one or two of them are overproduced [13].

Analytical, diagnostic and therapeutic context of ECs0097

• The truncated FtsA protein lacking domain 1C (FtsADelta1C) localizes in correctly placed division rings, together with FtsZ and ZipA, but does not interact with other FtsA molecules in the yeast two-hybrid assay, and fails to recruit FtsQ and FtsN into the division ring [14].

References