Disease relevance of ftsA

• The essential cell division genes ftsQ, ftsA and ftsZ map in a cluster of cell envelope genes located at two minutes on the Escherichia coli genetic map and appear to constitute an atypical operon [1].
• Thus, transcription of ftsA and ftsZ mimics their order of action in Caulobacter and proper transcription of ftsA has to be maintained for normal cell division and differentiation [2].
• Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein [3].
• Cell division of Klebsiella pneumoniae was inhibited on removal of ofloxacin, but no clear PAE was demonstrated with this species because once replication recommenced, the mean generation times of drug-treated cultures were much shorter than those of untreated controls [4].

High impact information on ftsA

• Cell division in bacteria is mediated by the tubulin-like protein FtsZ, which assembles into a structure known as the Z ring at the future site of cytokinesis [5].
• A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli [6].
• Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation [7].
• Cell division traps one or more plasmid copies in each daughter [8].
• Cell division normally follows the completion of each round of chromosome replication in Escherichia coli [9].

Chemical compound and disease context of ftsA

• Mutations in the ftsA gene of Escherichia coli conferred a higher resistance to lysis induced by penicillin or by a combination of cefsulodin and furazlocillin [10].
• Cell division by strains of Escherichia coli and Salmonella typhimurium is inhibited by 5-diazouracil (5-DU) [11].
• Synchronous cells of the thermosensitive division-defective Escherichia coli strain MACI (divA) divided at the restrictive temperature (42 degrees C) if they were allowed to grow at 42 degrees C for a certain period before protein synthesis was inhibited by adding chloramphenicol (CAP) or rifampicin [12].

Biological context of ftsA

• Structure and expression of the cell division genes ftsQ, ftsA and ftsZ [1].
• DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units [13].
• Missense mutations were determined in the ftsA and ftsW products yielding amino-acid replacements at conserved positions [14].
• Transcription of ftsA by P(A) is sufficient for cell viability, but is not sufficient for normal cell division [2].
• DNA fragments encoding the ftsA gene were subcloned into plasmids downstream of a lac promoter or a tac promoter [15].

Anatomical context of ftsA

• Partially purified FtsA protein was obtained by solubilizing cellular inclusion bodies after overexpression of the ftsA gene for the purpose of raising monoclonal antibodies [16].
• Cell division and cell wall synthesis are tightly linked cellular processes for bacterial growth [14].
• Cell division in bacteria such as Escherichia coli entails changes in the radii of curvature of the invaginating cytoplasmic membrane which culminate in rearrangements of its monolayers [17].

Associations of ftsA with chemical compounds

• After cloning the ftsA region from a strain containing the spoIIN279(ts) mutation we found that this mutation converts the ninth residue of the FtsA protein from serine to asparagine [18].
• Sublethal Concentrations of the Aminoglycoside Amikacin Interfere with Cell Division without Affecting Chromosome Dynamics [19].
• Cell division in particular appears very sensitive to the level of cell Ca(2+), with the frequency of division clearly reduced by EGTA and by verapamil [20].
• This chloramphenicol treatment of ftsA-3 filaments (previously designated at divA) does not induce cell division but does induce cell lysis [21].

Physical interactions of ftsA

• The observation that the termination codon of ftsQ overlaps with a potential initiation codon for ftsA suggested that these two genes may be translationally coupled when transcription is initiated upstream of the ftsQ coding sequence [13].

Regulatory relationships of ftsA

• We have previously shown that ftsA can be expressed from a weak promoter located within the ftsQ gene (Robinson et al., J. Bacteriol. 160:546-555, 1984) [22].

Other interactions of ftsA

• The promoter, ftsA1p, located in the ftsQ coding sequence, co-regulates ftsA and ftsZ [23].
• The new constrictions were blunt in ftsQ and more pronounced in ftsA and pbpB filaments, which also had elongated median constrictions [24].
• Also located on this DNA fragment is the 3' end of the ftsA gene and the 5' end of the envA gene [25].
• Cell division defects in Escherichia coli deficient in the multidrug efflux transporter AcrEF-TolC [26].

Analytical, diagnostic and therapeutic context of ftsA

• Sequence analysis of the dds gene and four other open reading frames upstream of ftsA revealed no significant homology to other known genes [27].

References