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RodZ, a new player in bacterial cell morphogenesis.

Gerdes K - EMBO J. (2009)

View Article: PubMed Central - PubMed

Affiliation: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK. kenn.gerdes@ncl.ac.uk

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Three different laboratories have now identified a new morphogenetic factor widely conserved in bacteria... The protein, RodZ, is required for assembly of the actin cytoskeleton MreB that controls cell wall synthesis and cell shape... Hironori Niki's group screened the Keio strain collection of gene deletions and thereby identified a novel gene, rodZ (yfgA) that is required to maintain proper cell shape... Cells lacking the rodZ gene were round or otherwise misshapen and exhibited a highly reduced growth rate... In that model, cell width is maintained by the MreBCD and PBP2/RodA complexes... Overproduction of RodZ resulted in an increased cell length with little or no change of cell width, consistent with the model... Piet de Boer's group identified rodZ by screening for the requirement for extra FtsZ, as it was known that increased FtsZ levels rescue the lack of other cell shape determinants (i.e. MreB and PBP2)... They also found that rodZ- cells exhibited a cold-sensitive phenotype... At low temperatures, the cells were non-dividing large and misshapen spheres... RodZ is a remarkable multidomain protein that, similar to MreB, forms helical structures associated with the cell membrane (Figure 1)... These results suggest a scenario in which RodZ interacts with components of the MreBCD–MrdAB (PBP2–RodA) machinery at either side of the membrane and that one of these interactions is sufficient to incorporate the JM domain into the MreB helix and thereby confer cell shape maintenance. constructed a fully functional mreB∷mCherry sandwich fusion and obtained convincing evidence that the formation of MreB and RodZ helices were interdependent, that is, both proteins were required for the helical structures to form... Supporting the view of, the subcellular localization pattern of RodZ depended on MreB and furthermore corresponded to active sites of peptidoglycan synthesis... In summary, all three papers identified a new, highly conserved morphogenetic factor and thereby have opened new possibilities in the difficult but essential analysis of the bacterial cell wall puzzle.

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Schematic diagram that visualizes the interactions between RodZ and the MreBCD–MrdAB (PBP2 RodA) complexes of E. coli. RodZ is shown as a vertical bar with four domains. The HTH domain (magenta) mediates interaction with MreB, whereas the juxta-membrane (JM) domain (+++) is in close contact with the negatively charged membrane phospholipids and serves to configure MreB in its helix-like appearance. P is the periplasmic part of RodZ that interacts with as yet unknown components in the periplasm. MreB is shown as a yellow helix beneath the inside of the inner membrane (IM) that interacts with MreC (red helix). MreC, in turn, interacts with PBP2 (green) and different OMPs. PP, periplasm; OM, outer membrane; PG, peptidoglycan layer; D, MreD in the IM; A, RodA in the IM.
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f1: Schematic diagram that visualizes the interactions between RodZ and the MreBCD–MrdAB (PBP2 RodA) complexes of E. coli. RodZ is shown as a vertical bar with four domains. The HTH domain (magenta) mediates interaction with MreB, whereas the juxta-membrane (JM) domain (+++) is in close contact with the negatively charged membrane phospholipids and serves to configure MreB in its helix-like appearance. P is the periplasmic part of RodZ that interacts with as yet unknown components in the periplasm. MreB is shown as a yellow helix beneath the inside of the inner membrane (IM) that interacts with MreC (red helix). MreC, in turn, interacts with PBP2 (green) and different OMPs. PP, periplasm; OM, outer membrane; PG, peptidoglycan layer; D, MreD in the IM; A, RodA in the IM.

Mentions: It is not yet understood how bacteria determine their shape. Almost all bacteria are surrounded by a giant cell wall polymer called peptidoglycan that gives shape to the cells and is an important target of antibiotics. Thus, one main aim is to understand the highly complex enzymatic machinery that synthesizes peptidoglycan and how its activity is coordinated with cell growth and division. The rod-shaped bacteria Escherichia coli and Bacillus subtilis and the curved Caulobacter crescentus have been used extensively as models in the study of cell morphogenesis. A paradigm has emerged in which the essential actin homologue MreB, discovered by Masaaki Wachi many years ago (Wachi et al, 1987), is a key player. In the beginning of the decade, it was shown that MreB of B. subtilis forms helical structures beneath the cell surface and that these structures are required to maintain cell shape (Jones et al, 2001). Later studies confirmed that MreBs of E. coli and C. crescentus (Kruse et al, 2003; Figge et al, 2004) played a similar role. MreB interacts with MreC and MreD and these latter proteins are also essential to cell shape maintenance (Kruse et al, 2005). MreB and MreC are inner membrane proteins much less abundant than MreB (Wachi et al, 2006). Bacterial two-hybrid analyses and pull-down experiments showed that MreC interacts with the penicillin-binding proteins that synthesize the cell wall and therefore are cell shape determinants (Divakaruni et al, 2005, 2007; van den Ent et al, 2006). These results raised the possibility that the MreB filaments interact with MreCD complexes located in the inner cell membrane and thereby control the activity of the external cell wall-synthesizing protein complexes in space and time. This conjecture was supported by the observation that MreC forms helical structures that alternate with the MreB helices (Dye et al, 2005). This simple model is shown schematically in Figure 1.


RodZ, a new player in bacterial cell morphogenesis.

Gerdes K - EMBO J. (2009)

Schematic diagram that visualizes the interactions between RodZ and the MreBCD–MrdAB (PBP2 RodA) complexes of E. coli. RodZ is shown as a vertical bar with four domains. The HTH domain (magenta) mediates interaction with MreB, whereas the juxta-membrane (JM) domain (+++) is in close contact with the negatively charged membrane phospholipids and serves to configure MreB in its helix-like appearance. P is the periplasmic part of RodZ that interacts with as yet unknown components in the periplasm. MreB is shown as a yellow helix beneath the inside of the inner membrane (IM) that interacts with MreC (red helix). MreC, in turn, interacts with PBP2 (green) and different OMPs. PP, periplasm; OM, outer membrane; PG, peptidoglycan layer; D, MreD in the IM; A, RodA in the IM.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2637339&req=5

f1: Schematic diagram that visualizes the interactions between RodZ and the MreBCD–MrdAB (PBP2 RodA) complexes of E. coli. RodZ is shown as a vertical bar with four domains. The HTH domain (magenta) mediates interaction with MreB, whereas the juxta-membrane (JM) domain (+++) is in close contact with the negatively charged membrane phospholipids and serves to configure MreB in its helix-like appearance. P is the periplasmic part of RodZ that interacts with as yet unknown components in the periplasm. MreB is shown as a yellow helix beneath the inside of the inner membrane (IM) that interacts with MreC (red helix). MreC, in turn, interacts with PBP2 (green) and different OMPs. PP, periplasm; OM, outer membrane; PG, peptidoglycan layer; D, MreD in the IM; A, RodA in the IM.
Mentions: It is not yet understood how bacteria determine their shape. Almost all bacteria are surrounded by a giant cell wall polymer called peptidoglycan that gives shape to the cells and is an important target of antibiotics. Thus, one main aim is to understand the highly complex enzymatic machinery that synthesizes peptidoglycan and how its activity is coordinated with cell growth and division. The rod-shaped bacteria Escherichia coli and Bacillus subtilis and the curved Caulobacter crescentus have been used extensively as models in the study of cell morphogenesis. A paradigm has emerged in which the essential actin homologue MreB, discovered by Masaaki Wachi many years ago (Wachi et al, 1987), is a key player. In the beginning of the decade, it was shown that MreB of B. subtilis forms helical structures beneath the cell surface and that these structures are required to maintain cell shape (Jones et al, 2001). Later studies confirmed that MreBs of E. coli and C. crescentus (Kruse et al, 2003; Figge et al, 2004) played a similar role. MreB interacts with MreC and MreD and these latter proteins are also essential to cell shape maintenance (Kruse et al, 2005). MreB and MreC are inner membrane proteins much less abundant than MreB (Wachi et al, 2006). Bacterial two-hybrid analyses and pull-down experiments showed that MreC interacts with the penicillin-binding proteins that synthesize the cell wall and therefore are cell shape determinants (Divakaruni et al, 2005, 2007; van den Ent et al, 2006). These results raised the possibility that the MreB filaments interact with MreCD complexes located in the inner cell membrane and thereby control the activity of the external cell wall-synthesizing protein complexes in space and time. This conjecture was supported by the observation that MreC forms helical structures that alternate with the MreB helices (Dye et al, 2005). This simple model is shown schematically in Figure 1.

View Article: PubMed Central - PubMed

Affiliation: Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK. kenn.gerdes@ncl.ac.uk

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

Three different laboratories have now identified a new morphogenetic factor widely conserved in bacteria... The protein, RodZ, is required for assembly of the actin cytoskeleton MreB that controls cell wall synthesis and cell shape... Hironori Niki's group screened the Keio strain collection of gene deletions and thereby identified a novel gene, rodZ (yfgA) that is required to maintain proper cell shape... Cells lacking the rodZ gene were round or otherwise misshapen and exhibited a highly reduced growth rate... In that model, cell width is maintained by the MreBCD and PBP2/RodA complexes... Overproduction of RodZ resulted in an increased cell length with little or no change of cell width, consistent with the model... Piet de Boer's group identified rodZ by screening for the requirement for extra FtsZ, as it was known that increased FtsZ levels rescue the lack of other cell shape determinants (i.e. MreB and PBP2)... They also found that rodZ- cells exhibited a cold-sensitive phenotype... At low temperatures, the cells were non-dividing large and misshapen spheres... RodZ is a remarkable multidomain protein that, similar to MreB, forms helical structures associated with the cell membrane (Figure 1)... These results suggest a scenario in which RodZ interacts with components of the MreBCD–MrdAB (PBP2–RodA) machinery at either side of the membrane and that one of these interactions is sufficient to incorporate the JM domain into the MreB helix and thereby confer cell shape maintenance. constructed a fully functional mreB∷mCherry sandwich fusion and obtained convincing evidence that the formation of MreB and RodZ helices were interdependent, that is, both proteins were required for the helical structures to form... Supporting the view of, the subcellular localization pattern of RodZ depended on MreB and furthermore corresponded to active sites of peptidoglycan synthesis... In summary, all three papers identified a new, highly conserved morphogenetic factor and thereby have opened new possibilities in the difficult but essential analysis of the bacterial cell wall puzzle.

Show MeSH