Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus

Hayashi, Ikuko

doi:10.1093/emboj/20.8.1819

Cited by 120 publications

(161 citation statements)

References 60 publications

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“…Both ATP and ATP␥S are able to support this step although another ATP analogue, AMPPCP, does not. Interestingly, the structures of MinD with ADP or AMPPCP bound are identical, arguing that for MinD AMPPCP is a poor analogue of ATP (18). Also, we observed that MinD K16Q-bound ATP but was unable to bind to phospholipid vesicles.…”

Section: Discussionmentioning

confidence: 58%

“…The pitch of the MinD helix on the tubes was determined at 59 Å, a distance that can accommodate the long axis of a MinD monomer [a MinD monomer can be approximated as a rectangular box with a height of 57 Å and a length and depth of 35 Å; determined from Hayashi et al (18)]. Such a packed array of MinD cannot occur in vivo as there is insufficient MinD to coat half of the inner surface of the cell membrane (21).…”

Section: Discussionmentioning

confidence: 99%

“…Several mutations have been described that alter residues within the ATP binding pocket of MinD and inactivate MinD function (9,18). One such mutation results in a K16Q substitution in the Walker A motif.…”

Section: Mind K16q Is Deficient In Tube Formation and Binding To Phosmentioning

confidence: 99%

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Gogol

Lutkenhaus

2002

Proc. Natl. Acad. Sci. U.S.A.

268

380

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Section: Discussionmentioning

confidence: 58%

Section: Discussionmentioning

confidence: 99%

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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Gogol

Lutkenhaus

2002

Proc. Natl. Acad. Sci. U.S.A.

268

380

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“…To examine the importance of the C-terminal region in membrane localization of MinD, we aimed to delete as much of the C terminus as possible without perturbing the 3D fold of the protein. In all three MinD structures solved to date, the final structural element preceding the disordered C-terminal region is an ␣-helix (designated ␣11 in the two Pyrococcus structures) (16,17). Sequence alignments show that the C terminus of ␣11 corresponds to Leu-247 of E. coli MinD.…”

Section: The C-terminal Region Of Mind Is Essential For Membrane Attamentioning

confidence: 99%

“…Crystal structures have been determined for presumptive MinD homologs from the hyperthermophilic archaeons Archaeoglobus fulgidus (15), Pyrococcus furiosus (16), and Pyrococcus horikoshii (17). Unfortunately, these structures provide little insight into the mechanism by which MinD associates with the membrane.…”

mentioning

confidence: 99%

Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts

Szeto

Rowland

Rothfield

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

221

246

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MinD is a widely conserved ATPase that has been demonstrated to play a pivotal role in selection of the division site in eubacteria and chloroplasts. It is a member of the large ParA superfamily of ATPases that are characterized by a deviant Walker-type ATP-binding motif. MinD localizes to the cytoplasmic face of the inner membrane in Escherichia coli, and its association with the inner membrane is a prerequisite for membrane recruitment of the septation inhibitor MinC. However, the mechanism by which MinD associates with the membrane has proved enigmatic; it seems to lack a transmembrane domain and the amino acid sequence is devoid of hydrophobic tracts that might predispose the protein to interaction with lipids. In this study, we show that the extreme C-terminal region of MinD contains a highly conserved 8-to 12-residue sequence motif that is essential for membrane localization of the protein. We provide evidence that this motif forms an amphipathic helix that most likely mediates a direct interaction between MinD and membrane phospholipids. A model is proposed whereby the membrane-targeting motif mediates the rapid cycles of membrane attachment-release-reattachment that are presumed to occur during pole-to-pole oscillation of MinD in E. coli. D uring vegetative growth, most bacteria form a division septum at the center of the cell by coordinated ingrowth of the cytoplasmic membrane, the rigid murein (peptidoglycan) layer, and, in Gram-negative bacteria, the outer membrane of the cell envelope (1). In the rod-shaped bacterium Escherichia coli, placement of the division septum is negatively regulated by the three proteins encoded by the minB operon: MinC, MinD, and MinE (2, 3). MinC and MinD act in concert to form a global division inhibitor whose activity is restricted to polar sites by MinE (2). Studies of GFP-labeled Min proteins have revealed that they undergo a complex bipolar oscillation that causes the time-averaged concentration of the MinC-MinD division inhibitor to be lowest at midcell (4-8). This dynamic distribution of MinC-MinD makes midcell the preferred site for construction of a circumferential ring of polymerized FtsZ, which is the initiating event in bacterial cytokinesis (9).MinD is the best conserved and most widely distributed of the Min proteins, being found in all domains of life (eubacteria, archaea, and eukaryotes). It is a member of the ParA superfamily of ATPases, most of which (apart from the MinD subgroup) are involved in plasmid or chromosome partitioning (10-12). The ATPase activity of MinD is presumed to provide the driving force for pole-to-pole oscillation of the MinC-MinD division inhibitor (13,14). This activity is stimulated by MinE but only in the presence of phospholipids (13,14). MinD is a peripheral membrane protein (10), and its association with the inner membrane is a prerequisite for subsequent recruitment of both MinC and MinE to the membrane. However, the mechanism by which MinD associates with the inner membrane and subsequently recruits MinC and MinE remains enig...

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CODehydrogenase and Acetyl‐CoASynthase Assembly

Dobbek

2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Ni,Fe‐containing carbon monoxide dehydrogenases (CODHs) and acetyl‐CoA synthases (ACSs) are ubiquitous among anaerobic bacteria and archaea. CODHs catalyze the reversible reduction of CO 2 with two electrons and two protons to CO and water. ACSs catalyze the reversible condensation of CO, coenzyme A, and a methyl cation to acetyl‐CoA, and both enzymes can occur in a monofunctional or as a stable bifunctional complex. Compared to what is known about the maturation of other Ni‐containing enzymes, how CODH and ACS mature is just beginning to emerge. Despite differences in active‐site metal content (CODH: 1xNi, 4xFe; ACS: 2xNi, 4xFe), architecture (CODH: Ni integrated in a NiFe 3 S 4 cubanoidal subcluster; ACS: two Ni next to a [4Fe4S] cluster), active‐site accessibility, and protein fold, both Ni,Fe‐clusters are matured by homologous ATPases of the MinD/Mrp‐family called CooC (CODH maturation) and AcsF (ACS maturation). CooC sustains the ATP‐dependent Ni insertion into the active‐site cluster of CODHs in the presence of physiological nickel concentrations. CooC can bind nickel at a GCXC motif in the dimer interface and ADP/ATP binding changes the coordination of nickel. AcsF forms a tight complex with Ni‐free ACS, together creating a binding platform for two nickel ions. The Ni‐loaded ACS–AcsF complex remains inactive until MgATP is added to it, resulting in fully active ACS. Details of the mechanisms and structures known to date are discussed in the chapter.

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Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus

Cited by 120 publications

References 60 publications

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts

CODehydrogenase and Acetyl‐CoASynthase Assembly

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