Movement Dynamics of Divisome and Penicillin-Binding Proteins (PBPs) in Cells of <i>Streptococcus pneumoniae</i>

Perez, Amilcar J.; Cesbron, Yann; Shaw, Sidney L.; Villicana, Jesus Bazan; Tsui, Ho‐Ching Tiffany; Boersma, Michael J.; Ye, Ziyun A.; Tovpeko, Yanina; Dekker, Cees; Holden, Séamus; Winkler, Malcolm E.

doi:10.1101/429217

Cited by 2 publications

(2 citation statements)

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“…The copyright holder for this preprint this version posted December 20, 2020. ; https://doi.org/10.1101/2020.12.18.423453 doi: bioRxiv preprint of cross links in PG by removing the terminal D-Ala residues of pentapeptides (5)(6)(7). It is widely acknowledged that PBP2b is an essential part of the elongasome and PBP2x is an essential part of the divisome (8)(9)(10). The Shape Elongation Division and Sporulation (SEDS) proteins RodA and FtsW have emerged as the main TG enzymes during PG production, working alongside the TP enzymes PBP2b and PBP2x, respectively.…”

Section: Introductionmentioning

confidence: 99%

EloR Interacts with the Lytic Transglycosylase MltG at Midcell in Streptococcus pneumoniae R6

et al. 2021

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The ellipsoid shape of Streptococcus pneumoniae is determined by the synchronized actions of the elongasome and the divisome, which have the task of creating a protective layer of peptidoglycan (PG) enveloping the cell membrane. The elongasome is necessary for expanding PG in the longitudinal direction whereas the divisome synthesizes the PG that divides one cell into two. Although there is still little knowledge about how these two modes of PG synthesis are coordinated, it was recently discovered that two RNA-binding proteins called EloR and KhpA are part of a novel regulatory pathway controlling elongation in S. pneumoniae. EloR and KhpA form a complex that work closely with the Ser/Thr kinase StkP to regulate cell elongation. Here, we have further explored how this regulation occur. EloR/KhpA is found at midcell, a localization fully dependent on EloR. Using a bacterial two-hybrid assay we probed EloR against several elongasome proteins and found an interaction with the lytic transglycosylase homolog MltG. By using EloR as bait in immunoprecipitation assays, MltG was pulled down confirming that they are part of the same protein complex. Fluorescent microscopy demonstrated that the Jag domain of EloR is essential for EloR’s midcell localization and its interaction with MltG. Since MltG is found at midcell independent of EloR, our results suggest that MltG is responsible for recruitment of the EloR/KhpA complex to the division zone to regulate cell elongation. Importance Bacterial cell division has been a successful target for antimicrobial agents for decades. How different pathogens regulate cell division is, however, poorly understood. To fully exploit the potential for future antibiotics targeting cell division, we need to understand the details of how the bacteria regulate and construct cell wall during this process. Here we have revealed that the newly identified EloR/KhpA complex, regulating cell elongation in S. pneumoniae, forms a complex with the essential peptidoglycan transglycosylase MltG at midcell. EloR, KhpA and MltG are conserved among many bacterial species and the EloR/KhpA/MltG regulatory pathway is most likely a common mechanism employed by many Gram-positive bacteria to coordinate cell elongation and septation.

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Section: Introductionmentioning

confidence: 99%

EloR Interacts with the Lytic Transglycosylase MltG at Midcell in Streptococcus pneumoniae R6

et al. 2021

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“…It is made The copyright holder for this preprint this version posted December 20, 2020. ; https://doi.org/10.1101/2020.12.18.423453 doi: bioRxiv preprint of cross links in PG by removing the terminal D-Ala residues of pentapeptides (5)(6)(7). It is widely acknowledged that PBP2b is an essential part of the elongasome and PBP2x is an essential part of the divisome (8)(9)(10). The Shape Elongation Division and Sporulation (SEDS) proteins RodA and FtsW have emerged as the main TG enzymes during PG production, working alongside the TP enzymes PBP2b and PBP2x, respectively.…”

Section: Introductionmentioning

confidence: 99%

EloR interacts with the lytic transglycosylase MltG at midcell inStreptococcus pneumoniaeR6

Winther

Kjos

Herigstad

et al. 2020

Preprint

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The ellipsoid shape of Streptococcus pneumoniae is determined by the synchronized actions of the elongasome and the divisome, which have the task of creating a protective layer of peptidoglycan (PG) enveloping the cell membrane. The elongasome is necessary for expanding PG in the longitudinal direction whereas the divisome synthesizes the PG that divides one cell into two. Although there is still little knowledge about how these two modes of PG synthesis are coordinated, it was recently discovered that two RNA-binding proteins called EloR and KhpA are part of a novel regulatory pathway controlling elongation in S. pneumoniae. EloR and KhpA form a complex that work closely with the Ser/Thr kinase StkP to regulate cell elongation. Here, we have further explored how this regulation occur. EloR/KhpA is found at midcell, a localization fully dependent on EloR. Using a bacterial two-hybrid assay we probed EloR against several elongasome proteins and found an interaction with the lytic transglycosylase homolog MltG. By using EloR as bait in immunoprecipitation assays, MltG was pulled down confirming that they are part of the same protein complex. Fluorescent microscopy demonstrated that the Jag domain of EloR is essential for EloR’s midcell localization and its interaction with MltG. Since MltG is found at midcell independent of EloR, our results suggest that MltG is responsible for recruitment of the EloR/KhpA complex to the division zone to regulate cell elongation.ImportanceBacterial cell division has been a successful target for antimicrobial agents for decades. How different pathogens regulate cell division is, however, poorly understood. To fully exploit the potential for future antibiotics targeting cell division, we need to understand the details of how the bacteria regulate and construct cell wall during this process. Here we have revealed that the newly identified EloR/KhpA complex, regulating cell elongation in S. pneumoniae, forms a complex with the essential peptidoglycan transglycosylase MltG at midcell. EloR, KhpA and MltG are conserved among many bacterial species and the EloR/KhpA/MltG regulatory pathway is most likely a common mechanism employed by many Gram-positive bacteria to coordinate cell elongation and septation.

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Movement Dynamics of Divisome and Penicillin-Binding Proteins (PBPs) in Cells of Streptococcus pneumoniae

Cited by 2 publications

References 59 publications

EloR Interacts with the Lytic Transglycosylase MltG at Midcell in Streptococcus pneumoniae R6

EloR Interacts with the Lytic Transglycosylase MltG at Midcell in Streptococcus pneumoniae R6

EloR interacts with the lytic transglycosylase MltG at midcell inStreptococcus pneumoniaeR6

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