Interaction of FtsA and PBP3 proteins in the Escherichia coli septum

Tormo, Antonio; Ayala, Juan A.; Pedro, Miguel A. de; Aldea, Martí; Vicente, Miguel

doi:10.1128/jb.166.3.985-992.1986

Cited by 88 publications

(59 citation statements)

References 34 publications

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“…Hence, it is possible that the C-terminal conserved region mediates the interaction of FtsZ and cell division protein(s), including FtsA, that couple the FtsZ ring to peptidoglycan biosynthesis. Indeed, one of the roles of FtsA may be to mediate the interaction between FtsZ and FtsI (PBP3) required for septal peptidoglycan synthesis (Tormo et al, 1986). However, there are a few Gram-negative bacteria, such as H. influenzae (Fleischmann et al, 1995) in which FtsZ does not contain the conserved C-terminal region even if some of the other cell division genes are present.…”

Section: Discussionmentioning

confidence: 99%

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Din

Quardokus

Sackett

et al. 1998

Molecular Microbiology

115

116

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SummaryThe cell division protein FtsZ is composed of three regions based on sequence similarity: a highly conserved N-terminal region of Ϸ320 amino acids; a variable spacer region; and a conserved C-terminal region of eight amino acids. We show that FtsZ mutants missing different C-terminal fragments have dominant lethal effects because they block cell division in Caulobacter crescentus by two different mechanisms. Removal of the C-terminal conserved region, the linker, and 40 amino acids from the end of the Nterminal conserved region (FtsZ⌬C281) prevents the localization or the polymerization of FtsZ. Because two-hybrid analysis indicates that FtsZ⌬C281 does not interact with FtsZ, we hypothesize that FtsZ⌬C281 blocks cell division by competing with a factor required for FtsZ localization or that it titrates a factor required for the stability of the FtsZ ring. The removal of 24 amino acids from the C-terminus of FtsZ (FtsZ⌬C485) causes a punctate pattern of FtsZ localization and affects its interaction with FtsA. This suggests that the conserved C-terminal region of FtsZ is required for proper polymerization of FtsZ in Caulobacter and for its interaction with FtsA.

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Section: Discussionmentioning

confidence: 99%

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Din

Quardokus

Sackett

et al. 1998

Molecular Microbiology

115

116

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“…One of the hypothetical roles of FtsA in division is to mediate an interaction between FtsZ in the cytoplasm and the septumspecific peptidoglycan synthetic machinery in the periplasm. PBP3, the cell division-specific peptidoglycan synthetase encoded byftsI, is one of the components of the peptidoglycan synthetic machinery probably interacting directly with ftsA (39). FtsN and FtsQ may be additional components.…”

Section: Resultsmentioning

confidence: 99%

“…It has both transglycosylase and transpeptidase activities, and the latter can be specifically inhibited by certain P-lactams (38). An interaction between PBP3 and FtsA has been previously suggested on the basis of the ability of one allele of ftsA to affect the binding of a P-lactam to PBP3 (39). Although little is known about the action of the ftsQ gene product, our previous observations suggest that it functionally interacts with FtsZ, FtsA, and PBP3 (14).…”

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confidence: 96%

Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)

1993

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“…It has been proposed that FtsA is a component of a membrane-associated complex (septator or divisome), which would include periplasmic, transmembrane, and cytoplasmic proteins acting coordinately to perform septation (27,35). Genetic analysis suggests that FtsA may interact, directly or indirectly, with other cell division proteins, such as FtsZ, PBP3, FtsQ, and FtsN (9,10,24,33,34). The FtsZ/FtsA ratio is important for cell division, and the localization of FtsA to a central position along the cell length depends on the formation of the FtsZ ring (1,8,11,15,23).…”

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confidence: 99%

Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

et al. 2000

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The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of the ftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutation (Gayda et al., J. Bacteriol. 174:5362-5370, 1992), suggesting that an interaction of FtsA with itself might play a role in its function. The existence of such an interaction was demonstrated using the yeast two-hybrid system and a protein overlay assay. Even these short deletions are sufficient for impairing the interaction of the truncated FtsA forms with the wild-type protein in the yeast two-hybrid system. The existence of additional interactions between FtsA molecules, involving other domains, can be postulated from the interaction properties shown by the FtsA deletion mutant forms, because although unable to interact with the wild-type and with FtsA⌬1, they can interact with themselves and cross-interact with each other. The secondary structures of an extensive deletion, FtsA⌬27, and the wild-type protein are indistinguishable when analyzed by Fourier transform infrared spectroscopy, and moreover, FtsA⌬27 retains the ability to bind ATP. These results indicate that deletion of the carboxy-terminal 27 residues does not alter substantially the structure of the protein and suggest that the loss of biological function of the carboxy-terminal deletion mutants might be related to the modification of their interacting properties.FtsA is an essential cell division protein of Escherichia coli that is widely conserved in bacteria. Together with ftsZ, which codes for a GTPase analog of the eukaryotic tubulin, ftsA forms one of the most frequently conserved gene pairs among the cell division genes in the eubacteria. Based on sequence homology it has been proposed that FtsA belongs to the sugar kinase/hsp70/actin superfamily (4). This superfamily comprises several proteins with a common two-domain topology and the ability to bind and hydrolyze ATP. FtsA binds to columns of ATP-agarose and can be isolated from cells either as a phosphorylated or a nonphosphorylated form (29), but so far no other biochemical function has been described for this protein.FtsA is present both in the cytoplasm and in the cytoplasmic membrane (29), where it forms a structural part of the septum (32). It has been proposed that FtsA is a component of a membrane-associated complex (septator or divisome), which would include periplasmic, transmembrane, and cytoplasmic proteins acting coordinately to perform septation (27,35). Genetic analysis suggests that FtsA may interact, directly or indirectly, with other cell division proteins, such as FtsZ, PBP3, FtsQ, and FtsN (9,10,24,33,34). The FtsZ/FtsA ratio is important for cell division, an...

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Interaction of FtsA and PBP3 proteins in the Escherichia coli septum

Cited by 88 publications

References 34 publications

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)

Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

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