FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in <i>Escherichia coli</i>

Berezuk, Alison; Roach, Elyse J.; Seidel, Laura; Lo, Reggie Y.C.; Khursigara, Cezar M.

doi:10.1139/cjm-2019-0493

Cited by 13 publications

(5 citation statements)

References 52 publications

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“…E. coli RlpA lacks LT activity (due to the substitution of the catalytic aspartate with a serine) and is bound to the large (1329 amino acids), polytopic membrane protein FtsK of the divisome 38 , 59 . FtsK coordinates the essential function of chromosome segregation with cell division, and in this task, may structurally connect the cytoskeletal proteins to proteins of the divisome located in the periplasm, including the membrane-bound PBPs 60 , 61 . Deletion of RlpA from E. coli does not, however, give a recognizable phenotype 49 .…”

Section: Introductionmentioning

confidence: 99%

In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa

et al. 2022

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The protein networks of cell-wall-biosynthesis assemblies are largely unknown. A key class of enzymes in these assemblies is the lytic transglycosylases (LTs), of which eleven exist in P. aeruginosa. We have undertaken a pulldown strategy in conjunction with mass-spectrometry-based proteomics to identify the putative binding partners for the eleven LTs of P. aeruginosa. A total of 71 putative binding partners were identified for the eleven LTs. A systematic assessment of the binding partners of the rare lipoprotein A (RlpA), one of the pseudomonal LTs, was made. This 37-kDa lipoprotein is involved in bacterial daughter-cell separation by an unknown process. RlpA participates in both the multi-protein and multi-enzyme divisome and elongasome assemblies. We reveal an extensive protein-interaction network for RlpA involving at least 19 proteins. Their kinetic parameters for interaction with RlpA were assessed by microscale thermophoresis, surface-plasmon resonance, and isothermal-titration calorimetry. Notable RlpA binding partners include PBP1b, PBP4, and SltB1. Elucidation of the protein-interaction networks for each of the LTs, and specifically for RlpA, opens opportunities for the study of their roles in the complex protein assemblies intimately involved with the cell wall as a structural edifice critical for bacterial survival.

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Section: Introductionmentioning

confidence: 99%

In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa

et al. 2022

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“…Previous studies have found that several mutations in FtsA bypassed the requirement of a number of essential cell division proteins in E. coli , including ZipA (30), FtsK (31), and FtsN (32). Among these, FtsA R286W (FtsA*) was the first gain-of-function mutation found in E. coli , which allowed the survival of mutants lacking ZipA (Δ zipA ) or FtsK (Δ ftsK ) (30, 31, 33). Additionally, FtsA I143L (34) and FtsA E124A (32) weakly bypassed the requirement of FtsN.…”

Section: Resultsmentioning

confidence: 99%

A unique cell division protein critical for the assembly of the bacterial divisome

Chu

Wang

Zhu

et al. 2023

Preprint

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Identification of novel essential bacterial genes is important for not only the understanding of their cell biology but also the development of new antimicrobials. Here we report a previously unrecognized core component of the Acinetobacter baumannii divisome. Our results reveal that the protein, termed Aeg1 interacts with multiple cell division proteins, including FtsN, which is required for components of the divisome to localize to the midcell. We demonstrate that the FtsAE202K and FtsBE65A mutants effectively bypassed the need of Aeg1 by A. baumannii, so did the activation variants FtsWM254I and FtsWS274G. Our results suggest that Aeg1 is a cell division protein that arrives at the division site to initiate cell division by recruiting FtsN, which activates FtsQLB and FtsA to induces the septal peptidoglycan synthase FtsWI. The discovery of the new essential cell division protein has provided a new target for the development of antibacterial agents.

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“…Because of its important role in DNA segregation and cytokinesis FtsK mutations have severe phenotypes. In E. coli a loss of FtsK can be compensated by a suppressor mutation in FtsA (51). Although our Tn-Seq screen identified several transposon insertions into the FtsK gene in wild type background, we were unable to construct a clean deletion of the gene.…”

Section: Discussionmentioning

confidence: 99%

Deletion of SMC renders FtsK essential inCorynebacterium glutamicum

Peng,

Giacomelli,

Meyer

et al. 2023

Preprint

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Structural maintenance of chromosomes (SMC) are ubiquitously distributed proteins involved in chromosome organization. Deletion of smc causes severe growth phenotypes in many organisms. Surprisingly, smc can be deleted inCorynebacterium glutamicum, a member of the Actinomycetota phylum, without any apparent growth phenotype. Earlier work has shown that SMC inC. glutamicumis loaded in a ParB-dependent fashion to the chromosome and functions in replichore cohesion. The unexpected absence of a growth phenotype in the smc mutant prompted us to screen for unknown synthetic interactions withinC. glutamicum. Therefore, we generated a high-density Tn-5 library based on wild-type and smc-deletedC. glutamicumstrains. The transposon sequencing (Tn-seq) data revealed that the DNA-translocase FtsK is essential in a smc deletion strain. FtsK localized to the septa and cell poles in wild type cells, however deletion of smc resulted in a decreased polar FtsK localization. Single-particle tracking analysis further suggests that prolonged FtsK complex activity is both required and sufficient to make up for the absence of SMC, thus achieving efficient chromosome segregation inC. glutamicum. Further, single molecule dynamics of FtsK is influenced, albeit indirectly, by DNA-loaded SMC. Deletion of ParB results in an increased of both SMC and FtsK mobility. While the first change agrees with previous data that show how ParB is essential for SMC loading on DNA, the latter suggests that FtsK mobility is affected in cells with defects in chromosome organization. Based on our data we propose a simple, yet efficient mechanism for efficient DNA segregation inC. glutamicum, even in absence of SMC proteins.

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FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli

Cited by 13 publications

References 52 publications

In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa

In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa

A unique cell division protein critical for the assembly of the bacterial divisome

Deletion of SMC renders FtsK essential inCorynebacterium glutamicum

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