The N Terminus of MinD Contains Determinants Which Affect Its Dynamic Localization and Enzymatic Activity

Szeto, Jason; Acharya, Sudeep; Eng, Nelson F.; Dillon, Jo-Anne R.

doi:10.1128/jb.186.21.7175-7185.2004

Cited by 7 publications

(8 citation statements)

References 43 publications

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“…Key domains previously shown to be crucial for Min protein function and dynamics in E. coli were identified in all three predicted S. elongatus structures. MinD possessed a highly conserved N-terminal Walker Atype ATPase domain, Switch I and Switch II domains for binding MinC, and key residues L48, E53, and N222 (L48, E53 and N213 in S. elongatus) important for interaction with MinE (Zhou and Lutkenhaus, 2004;Szeto et al, 2004;Zhou et al, 2005) (Supporting Information Fig. 1C) (Hu and Lutkenhaus, 2000).…”

Section: Resultsmentioning

confidence: 99%

Robust Min‐system oscillation in the presence of internal photosynthetic membranes in cyanobacteria

MacCready

Schossau

Osteryoung

et al. 2016

Molecular Microbiology

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The oscillatory Min system of Escherichia coli defines the cell division plane by regulating the site of FtsZ-ring formation and represents one of the best-understood examples of emergent protein self-organization in nature. The oscillatory patterns of the Min-system proteins MinC, MinD and MinE (MinCDE) are strongly dependent on the geometry of membranes they bind. Complex internal membranes within cyanobacteria could disrupt this self-organization by sterically occluding or sequestering MinCDE from the plasma membrane. Here, it was shown that the Min system in the cyanobacterium Synechococcus elongatus PCC 7942 oscillates from pole-to-pole despite the potential spatial constraints imposed by their extensive thylakoid network. Moreover, reaction-diffusion simulations predict robust oscillations in modeled cyanobacterial cells provided that thylakoid network permeability is maintained to facilitate diffusion, and suggest that Min proteins require preferential affinity for the plasma membrane over thylakoids to correctly position the FtsZ ring. Interestingly, in addition to oscillating, MinC exhibits a midcell localization dependent on MinD and the DivIVA-like protein Cdv3, indicating that two distinct pools of MinC are coordinated in S. elongatus. Our results provide the first direct evidence for Min oscillation outside of E. coli and have broader implications for Min-system function in bacteria and organelles with internal membrane systems.

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Section: Resultsmentioning

confidence: 99%

Robust Min‐system oscillation in the presence of internal photosynthetic membranes in cyanobacteria

MacCready

Schossau

Osteryoung

et al. 2016

Molecular Microbiology

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“…All Ng-MinE constructs were prepared using a slightly modified version of the previously published protocol (38). Briefly, one colony of freshly transformed BL21(DE3) was used to inoculate 50 mL of M9 minimal media containing 50 µg/mL kanamycin and 0.1% (w/v) 15 N-labeled ammonium chloride and 0.3% (w/v) glucose (either U- 13 C or natural abundance) as the sole nitrogen and carbon sources, respectively. The culture was grown overnight at 37 °C and used to inoculate 1 L of the same minimal media which was induced with 0.4 mM isopropyl β-D-thiogalactopyranoside when the OD 600 reached 0.6-0.8.…”

Section: Methodsmentioning

confidence: 99%

“…Backbone 15 N, 1 H N , 13 C R , 13 C β , and 13 CO chemical shift assignments were made on the wild-type Ng-MinE at pH 9.5 based on HNCACB, CBCA(CO)NH, HNCA, HN(CO)-CA, and HNCO experiments, and amide proton assignments were confirmed with a 15 N-edited NOESY utilizing a 100 ms mixing time (41,42). Protected regions were mapped onto the Ec-TSD structure (37; PDB accession number 1EV0), and figures were rendered in MolMol (43).…”

Section: Methodsmentioning

confidence: 99%

“…Although the pattern of cell division in the two cell types is different, studies with Min proteins from the bacillus E. coli and the coccus N. gonorrhoeae suggest that they perform analogous functions to ensure proper placement of the cell division plane ( , ). In both cases MinD and MinC localize to a polymeric subcellular coiled structure on the membrane at one end of the cell, creating a zone that is inhibitory to formation of the cytokinetic septum ( , ).…”

mentioning

confidence: 99%

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Conformation of the Cell Division Regulator MinE: Evidence for Interactions between the Topological Specificity and Anti-MinCD Domains

et al. 2006

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Symmetric division of Gram-negative bacteria depends on the combined action of three proteins that ensure correct positioning of the cell division septum, namely, MinC, MinD, and MinE. To achieve this function, MinC and MinD form a membrane-bound complex that blocks cell division at all potential sites. Opposing this inhibition is MinE, which interacts with MinD via its N-terminal anti-MinCD domain to site-specifically counter the action of the MinCD complex. The anti-MinCD domain has been proposed to bind MinD in a helical conformation; however, little is actually known about the structure of this functionally critical region. To understand how MinE can perform its anti-MinCD function, we have therefore investigated the conformation of the full-length MinE from Neisseria gonorrhoeae by solution NMR. Although solubility considerations required the use of sample conditions that limit the observation of amide resonances to regions that are protected from solvent exchange, backbone chemical shifts from both N- and C-terminal domains could be assigned. In contrast to previous models, secondary chemical shift analysis of these solvent-protected regions shows that parts of the N-terminal anti-MinCD domain are stably folded with many functionally important residues localizing to a beta-structure. In addition, this N-terminal domain may be interacting with the C-terminal topological specificity domain, since mutations made in one domain led to NMR spectral changes in both domains. The nonfunctional MinE mutant L22D showed even larger evidence of structural perturbations in both domains, with significant destabilization of the entire MinE structure. Overall, these results suggest that there is an intimate structural association between the anti-MinCD and topological specificity domains, allowing the functional properties of the two domains to be modulated through this interaction.

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“…In Escherichia coli, it has been shown that oscillation rates that are too slow can inhibit normal cell division, giving rise to elongated rods (11), whereas oscillation rates that are too fast fail to prevent division at the cell poles (4), leading to the generation of achromosomal minicells that cannot undergo further propagation (12). The chemical engine that drives this coordinated oscillation of Min proteins from pole to pole is powered by MinD-catalyzed hydrolysis of ATP (13,14), which is stimulated by interactions with MinE once MinD has bound to the cell membrane in a dimeric state (15)(16)(17)(18)(19). ATP hydrolysis stimulates the release of Min proteins from the cell membrane (19,20), freeing them to diffuse through the cytoplasm to establish a new zone that is inhibitory to formation of the cytokinetic septum at the opposite side of the cell.…”

mentioning

confidence: 99%

Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity

Ayed¹,

Cloutier

McLeod

et al. 2017

Journal of Biological Chemistry

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The bacterial cell division regulators MinD and MinE together with the division inhibitor MinC localize to the membrane in concentrated zones undergoing coordinated pole-to-pole oscillation to help ensure that the cytokinetic division septum forms only at the mid-cell position. This dynamic localization is driven by MinD-catalyzed ATP hydrolysis, stimulated by interactions with MinE's anti-MinCD domain. This domain is buried in the 6-β-stranded MinE "closed" structure, but is liberated for interactions with MinD, giving rise to a 4-β-stranded "open" structure through an unknown mechanism. Here we show that MinE-membrane interactions induce a structural change into a state resembling the open conformation. However, MinE mutants lacking the MinE membrane-targeting sequence stimulated higher ATP hydrolysis rates than the full-length protein, indicating that binding to MinD is sufficient to trigger this conformational transition in MinE. In contrast, conformational change between the open and closed states did not affect stimulation of ATP hydrolysis rates in the absence of membrane binding, although the MinD-binding residue Ile-25 is critical for this conformational transition. We therefore propose an updated model where MinE is brought to the membrane through interactions with MinD. After stimulation of ATP hydrolysis, MinE remains bound to the membrane in a state that does not catalyze additional rounds of ATP hydrolysis. Although the molecular basis for this inhibited state is unknown, previous observations of higher-order MinE self-association may explain this inhibition. Overall, our findings have general implications for Min protein oscillation cycles, including those that regulate cell division in bacterial pathogens.

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The N Terminus of MinD Contains Determinants Which Affect Its Dynamic Localization and Enzymatic Activity

Abstract: MinD is involved in regulating the

Cited by 7 publications

References 43 publications

Robust Min‐system oscillation in the presence of internal photosynthetic membranes in cyanobacteria

Robust Min‐system oscillation in the presence of internal photosynthetic membranes in cyanobacteria

Conformation of the Cell Division Regulator MinE: Evidence for Interactions between the Topological Specificity and Anti-MinCD Domains

Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity

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