GpsB Coordinates Cell Division and Cell Surface Decoration by Wall Teichoic Acids in Staphylococcus aureus

Hammond, Lauren R.; Sacco, M.; Khan, Sebastian J.; Spanoudis, Catherine M.; Hough-Neidig, Abigail; Chen, Yu; Eswara, Prahathees J.

doi:10.1128/spectrum.01413-22

Cited by 22 publications

(47 citation statements)

References 65 publications

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“…Lastly, by GFP tagging, we observed that both mutants localize to the division site similar to Sa GpsB-GFP (Fig. S4F) 12,15 . In summary, ΔMNN is less functional compared to ΔMAD in terms of causing growth inhibition on plate and cell enlargement phenotype, however both ΔMAD and ΔMNN mutants are able to localize to division sites.…”

Section: The Mad/mnn Insertion Is Critical For Gpsb Functionmentioning

confidence: 76%

“…shown in Fig. 2D, Bs GpsB-GFP localizes to the division site 8,9,15 and does not lead to filamentation upon overproduction (2.09 µm ± 0.49 µm; n=50), but Sa GpsB-GFP localizes, forms foci throughout the entire cell, and causes severe filamentation (22.83 µm ± 16.51 µm; n=21) 12 . However, ΔMAD and ΔMNN Sa GpsB-GFP do not cause filamentation (2.13 µm ± 0.44 µm and 2.10 µm ± 0.43 µm respectively; n=50)…”

Section: The Mad/mnn Insertion Is Critical For Gpsb Functionmentioning

confidence: 89%

“…The protein was stored at -80 °C in the storage buffer (20 mM Tris-HCl pH 8.0, 200 mM NaCl). The purity of the protein was determined by SDS-PAGE as >95% 15. N-labelled GpsB (1-70) for NMR spectroscopy was expressed in the same way, but in minimal media containing 15 N NH4Cl and 12 C glucose as the source of nitrogen and carbon, respectively, supplemented with MgSO4, CaCl2, and trace metals.…”

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confidence: 99%

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Staphylococcus aureusFtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB

Sacco

Hammond

Noor

et al. 2022

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Bacterial cell division is a tightly regulated process that requires the formation of a dynamic multi-protein complex. In the Firmicutes phylum, GpsB is a membrane associated protein that coordinates peptidoglycan synthesis for cell growth and division. Although GpsB has been studied in several organisms, the structure, function, and interactome of Staphylococcus aureus GpsB is largely uncharacterized, despite being reported as uniquely essential for growth in this clinically relevant bacterium. To address this knowledge gap, we solved the crystal structure of the N-terminal domain of S. aureus GpsB. This structure reveals an atypical asymmetric dimer, and major conformational flexibility that can be mapped to a hinge region formed by a three-residue insertion exclusive to Staphylococci. When this three-residue insertion is excised, its thermal stability increases, and the mutant no longer produces a previously reported lethal phenotype when overexpressed in Bacillus subtilis. Furthermore, we provide the first biochemical, biophysical, and crystallographic evidence that the N-terminal domain of GpsB binds not only PBP4, but also FtsZ, through a conserved recognition motif located on their C-terminus, thus linking peptidoglycan synthesis with cell division. Taken together, the unique structure of S. aureus GpsB and its direct interaction with FtsZ/PBP4 provide deeper insight into the central role of GpsB in S. aureus cell division.

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Section: The Mad/mnn Insertion Is Critical For Gpsb Functionmentioning

confidence: 76%

Section: The Mad/mnn Insertion Is Critical For Gpsb Functionmentioning

confidence: 89%

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confidence: 99%

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Staphylococcus aureusFtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB

Sacco

Hammond

Noor

et al. 2022

Preprint

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“…This shows that SepIVA is not associated with primarily with curved membranes like other DivIVA proteins. Other described DivIVA proteins have been shown to have functions in promoting polar elongation (Kang et al ., 2008; Letek et al ., 2008; Hempel et al ., 2008; Melzer et al ., 2018), helping to inhibit cell division (Marston and Errington, 1999; Eswara et al ., 2018) and/or to bind and regulate transcription factors (Eswaramoorthy et al ., 2014), cell wall enzymes (Cleverley et al ., 2019), cell division regulators (Eswara et al ., 2018), and an envelope saccharide transporter (Hammond et al ., 2022). None of these DivIVA proteins are essential for cell division, as SepIVA is (Wu et al ., 2018).…”

Section: Discussionmentioning

confidence: 99%

“…S1). DivIVA homologs are often involved in recruitment of other proteins to cell poles or septa (Marston and Errington, 1999; Halbedel and Lewis, 2019; Hammond et al ., 2019; Hammond et al ., 2021). However, none of the confirmed interactors of DivIVA-domain proteins interact with residues that are conserved in SepIVA (Fig.…”

Section: Introductionmentioning

confidence: 99%

Arginine methylation sites on SepIVA help balance elongation and septation of the cell wall inMycobacterium smegmatis

Freeman

Tembiwa

Brenner

et al. 2021

Preprint

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Growth of mycobacterial cells requires successful coordination between elongation and division of the cell wall. However, it is not clear which factors directly mediate this coordination. Here, we studied the function and post-translational modification of an essential division factor, SepIVA, in Mycobacterium smegmatis. We find that SepIVA is arginine methylated, and that these modifications alter both division and polar elongation of Msmeg. Furthermore, SepIVA impacts the localization of MurG. Polar localization of MurG correlates with polar elongation in arginine methylation mutants of sepIVA. These results establish SepIVA as a regulator of both elongation and division, and characterize a physiological role for protein arginine methylation for the first time in bacteria.

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The cell cycle of Staphylococcus aureus: An updated review

et al. 2022

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As bacteria proliferate, DNA replication, chromosome segregation, cell wall synthesis, and cytokinesis occur concomitantly and need to be tightly regulated and coordinated. Although these cell cycle processes have been studied for decades, several mechanisms remain elusive, specifically in coccus‐shaped cells such as Staphylococcus aureus . In recent years, major progress has been made in our understanding of how staphylococci divide, including new, fundamental insights into the mechanisms of cell wall synthesis and division site selection. Furthermore, several novel proteins and mechanisms involved in the regulation of replication initiation or progression of the cell cycle have been identified and partially characterized. In this review, we will summarize our current understanding of the cell cycle processes in the spheroid model bacterium S. aureus , with a focus on recent advances in the understanding of how these processes are regulated.

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GpsB Coordinates Cell Division and Cell Surface Decoration by Wall Teichoic Acids in Staphylococcus aureus

Abstract: Cytokinesis in bacteria involves an intricate orchestration of several key cell division proteins and other factors involved in building a robust cell envelope. Presence of teichoic acids is a signature characteristic of the Gram-positive cell wall.

Cited by 22 publications

References 65 publications

Staphylococcus aureusFtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB

Staphylococcus aureusFtsZ and PBP4 bind to the conformationally dynamic N-terminal domain of GpsB

Arginine methylation sites on SepIVA help balance elongation and septation of the cell wall inMycobacterium smegmatis

The cell cycle of Staphylococcus aureus: An updated review

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