Characterization of rodZ mutants: RodZ is not absolutely required for the cell shape and motility

Niba, Emma Tabe Eko; Li, Gaochi; Aoki, Kenji; Kitakawa, Madoka

doi:10.1111/j.1574-6968.2010.02014.x

Cited by 11 publications

(23 citation statements)

References 38 publications

(49 reference statements)

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“…It has been reported that selected isolates of motile pseudo-revertants of the rodZ deletion mutant recover their swarming ability (Niba et al ., 2010). The morphology of these revertants is reminiscent of our suppressors.…”

Section: Discussionmentioning

confidence: 99%

“…This pathway then contributes to the formation of several essential lipids involved in peptidoglycan synthesis. Because the amount of peptidoglycan is reduced in the rodZ mutant (Niba et al ., 2010), the integrity of the cell wall, including peptidoglycan, may be reduced. The reduction of integrity of the cell wall may result in cold sensitivity in the mutant.…”

Section: Discussionmentioning

confidence: 99%

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Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ‐deficient cells

Shiomi

Toyoda

Aizu

et al. 2013

Molecular Microbiology

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RodZ interacts with MreB and both factors are required to maintain the rod shape of Escherichia coli. The assembly of MreB into filaments regulates the subcellular arrangement of a group of enzymes that synthesizes the peptidoglycan (PG) layer. However, it is still unknown how polymerization of MreB determines the rod shape of bacterial cells. Regulatory factor(s) are likely to be involved in controlling the function and dynamics of MreB. We isolated suppressor mutations to partially recover the rod shape in rodZ deletion mutants and found that some of the suppressor mutations occurred in mreB. All of the mreB mutations were in or in the vicinity of domain IA of MreB. Those mreB mutations changed the property of MreB filaments in vivo. In addition, suppressor mutations were found in the periplasmic regions in PBP2 and RodA, encoded by mrdA and mrdB genes. Similar to MreB and RodZ, PBP2 and RodA are pivotal to the cell wall elongation process. Thus, we found that mutations in domain IA of MreB and in the periplasmic domain of PBP2 and RodA can restore growth and rod shape to ΔrodZ cells, possibly by changing the requirements of MreB in the process.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ‐deficient cells

Shiomi

Toyoda

Aizu

et al. 2013

Molecular Microbiology

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“…RodZ of Thermotoga maritima interacted with MreB probably providing a scaffold for the MreB filaments and the assembly of the lateral wall synthesizing machinery (van den Ent et al ., 2010). rodZ ( yfgA ) mutants of E. coli were growth deficient and had a spherical shape instead of the normal rod‐shape (Alyahya et al ., 2009; Bendezu et al ., 2009; Niba et al ., 2010). The S. coelicolor rodZ homologue sco5751 is located downstream of ftsK , which is involved in the segregation of chromosomal DNA during sporulation.…”

Section: Discussionmentioning

confidence: 99%

Proteins encoded by the mre gene cluster in Streptomyces coelicolor A3(2) cooperate in spore wall synthesis

Kleinschnitz

Heichlinger

Schirner

et al. 2011

Molecular Microbiology

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SummaryIt is still an open question how an intracellular cytoskeleton directs the synthesis of the peptidoglycan exoskeleton. In contrast to MreB of rod-shaped bacteria, which is essential for lateral cell wall synthesis, MreB of Streptomyces coelicolor has a role in sporulation. To study the function of the S. coelicolor mre gene cluster consisting of mreB, mreC, mreD, pbp2 and sfr, we generated non-polar replacement mutants. The individual mutants were viable and growth of substrate mycelium was not affected. However, all mutants produced enlarged spores, which frequently germinated prematurely and were sensitive to heat, high osmolarity and cell wall damaging agents. Protein-protein interaction assays by bacterial two-hybrid analyses indicated that the S. coelicolor Mre proteins form a spore wall synthesizing complex, which closely resembles the lateral wall synthesizing complex of rod-shaped bacteria. Screening of a genomic library identified several novel putative components of this complex. One of them (sco2097) was deleted. The Dsco2097 mutant formed sensitive spores with an aberrant morphology, demonstrating that SCO2097 is a new player in cell morphogenesis of Streptomyces. Our results suggest that all Mre proteins cooperate with the newly identified proteins in the synthesis of the thickened spore wall required to resist detrimental environmental conditions.

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“…Elimination of the kanamycin‐resistant cassette was carried out as previously described (Datsenko & Wanner ; Niba et al . ). The inducible yciB ( P ara ‐yciB ) together with araC and bla (Amp R ) was transferred from plasmid pBADs‐ yciB and integrated into the chromosome near the att λ site using λInCh as previously described (Boyd et al .…”

Section: Methodsmentioning

confidence: 97%

Escherichia coli inner membrane protein YciB interacts with ZipA that is important for cell division

Badaluddin

Kitakawa

2015

Genes to Cells

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Escherichia coli propagates by undergoing cycles of lateral elongation, septum formation and cell fission at the mid-cell. A large number of genes involved in these processes have been identified but it is likely others remain. A deletion mutant of yciB (∆yciB) is shorter in the cell length compared to wild type and on the other hand overexpression of yciB causes elongation of the cell. Furthermore, the septum localization of ZipA, an essential protein of cell division, is disturbed in a ∆yciB mutant.Purified YciB protein directly interacted with ZipA, which might indicate that YciB is involved in the cell envelope synthesis directed by ZipA in PBP3 independent manner.

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Characterization of rodZ mutants: RodZ is not absolutely required for the cell shape and motility

Cited by 11 publications

References 38 publications

Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ‐deficient cells

Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ‐deficient cells

Proteins encoded by the mre gene cluster in Streptomyces coelicolor A3(2) cooperate in spore wall synthesis

Escherichia coli inner membrane protein YciB interacts with ZipA that is important for cell division

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