Membrane Binding by MinD Involves Insertion of Hydrophobic Residues within the C-Terminal Amphipathic Helix into the Bilayer

Zhou, Huaijin; Lutkenhaus, Joe

doi:10.1128/jb.185.15.4326-4335.2003

Cited by 91 publications

(107 citation statements)

References 27 publications

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“…More strikingly, targeting of MinD, a bacterial protein involved, like mid1p, in the spatial regulation of cytokinesis, relies on a C-terminal amphipathic helix (22,40). This helix is highly similar in sequence to mid1p helix (KKGFLKRLF in Escherichia coli) and has been shown to bind to lipids by direct insertion of hydrophobic residues into the lipid bilayer (39,46). Moreover, it has been proposed that ATP-regulated accessibility of this helix may account for MinD reversible membrane association during its pole-to-pole oscillation cycles (39).…”

Section: Discussionmentioning

confidence: 99%

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C-Terminal Anchoring of mid1p to Membranes Stabilizes Cytokinetic Ring Position in Early Mitosis in Fission Yeast

Celton-Morizur

Bordes

Fraisier

et al. 2004

Molecular and Cellular Biology

120

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mid1p is a key factor for the central positioning of the cytokinetic ring in Schizosaccharomyces pombe. In interphase and early mitosis, mid1p forms a medial cortical band overlying the nucleus, which may represent a landmark for cytokinetic ring assembly. It compacts before anaphase into a tight ring with other cytokinetic ring components. We show here that mid1p binds to the medial cortex by at least two independent means. First, mid1p C-terminus association with the cortex requires a putative amphipathic helix adjacent to mid1p nuclear localization sequence (NLS), which is predicted to insert directly into the lipid bilayer. This association is stabilized by the polybasic NLS. mid1p mutated within the helix and the NLS forms abnormal filaments in early mitosis that are not properly anchored to the medial cortex. Misplaced rings assemble in late mitosis, indicating that mid1p C-terminus binding to membranes stabilizes cytokinetic ring position. Second, the N terminus of mid1p has the ability to associate faintly with the medial cortex and is sufficient to form tight rings. In addition, we show that mid1p oligomerizes. We propose that membrane-bound oligomers of mid1p assemble recruitment "platforms" for cytokinetic ring components at the medial cortex and stabilize the ring position during its compaction.Cytokinesis is the last event of the cell division cycle, which allows the physical separation of the two sister cells. One early and critical step in this process is the definition of the orientation of the plane of division, since a proper orientation, perpendicular to the spindle elongation axis, is crucial for a faithful segregation of chromosomes between sister cells. In addition, division plane orientation also controls cell shape, tissue organization, or cell fate during development. For instance, during Caenorhabditis elegans early development, reorientation of the plane of division by rotation of the mitotic spindle in P cells allows the formation of the germ cell lineage by inheritance of specific determinants concentrated at the posterior pole of the embryo (18).The fission yeast Schizosaccharomyces pombe offers a simple system for studying cytokinesis and division plane specification. Fission yeast cells have a well-defined rod shape and a stereotyped medial division to form symmetric daughter cells. The position of the division plane always coincides with the position of the nucleus, at the center in wild-type cells, or off the center in mutants with abnormal microtubules that are defective in nuclear positioning (12,35,41). This suggests that the nucleus or the microtubules play a major role in positioning the division plane.As in higher eukaryotes, cell division depends on the assembly of a cytokinetic ring containing actin and type II myosin, as well as many other components involved in the nucleation of F-actin and the shaping F-actin and myosin II filaments into a compact ring (for reviews, see references 16, 19, and 20). Several phases have been described during ring formation (44). Ten minu...

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Section: Discussionmentioning

confidence: 99%

“…2A). Since amphipathic helices can directly insert into lipid bilayers (1,17,22,26,38,39,40,46), we assayed the role of mid1p putative helix in cortical anchorage by substituting hydrophobic amino acids (F and L) by alanine ( Fig. 2A).…”

Section: The C Terminus Of Mid1p Contains Cortex-targeting Motifsmentioning

confidence: 99%

C-Terminal Anchoring of mid1p to Membranes Stabilizes Cytokinetic Ring Position in Early Mitosis in Fission Yeast

Celton-Morizur

Bordes

Fraisier

et al. 2004

Molecular and Cellular Biology

120

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“…The C-terminal region that comprises the MTS of the A. fulgidus MinD (determined in the absence of phospholipid) is also unstructured (24). The hydrophobic side chains of the amino acids on the nonpolar face of the amphipathic helix intercalate into the bilayer, thereby anchoring the protein to the membrane (203,226). The membrane association is then stabilized by polymerization of the membrane-bound MinD (203).…”

Section: The Mind/para Class Of Bacterial Cytoskeletal Proteinsmentioning

confidence: 99%

The Bacterial Cytoskeleton

Shih

Rothfield

2006

Microbiol Mol Biol Rev

243

220

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SUMMARY In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA group, that appears to be unique to bacteria. The cytoskeletal structures play important roles in cell division, cell polarity, cell shape regulation, plasmid partition, and other functions. The proteins self-assemble into filamentous structures in vitro and form intracellular ordered structures in vivo. In addition, there are a number of filamentous bacterial elements that may turn out to be cytoskeletal in nature. This review attempts to summarize and integrate the in vivo and in vitro aspects of these systems and to evaluate the probable future directions of this active research field.

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“…Hydrophobic residues within this helix mediate binding by inserting into the bilayer (38). Deletion of this helix or mutations that substitute charged residues for hydrophobic residues prevent MinD from binding to the membrane (35,38).…”

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confidence: 99%

The Switch I and II Regions of MinD Are Required for Binding and Activating MinC

Zhou

Lutkenhaus

2004

J Bacteriol

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MinD and MinC cooperate to form an efficient inhibitor of Z-ring formation that is spatially regulated by MinE. MinD activates MinC by recruiting it to the membrane and targeting it to a septal component. To better understand this activation, we have isolated loss-of-function mutations in minD and carried out site-directed mutagenesis. Many of these mutations block MinC-MinD interaction; however, they also prevent MinD self-interaction and membrane binding, suggesting that they affect nucleotide interaction or protein folding. Two mutations in the switch I region (MinD box) and one mutation in the switch II region had little affect on most MinD functions, such as MinD self-interaction, membrane binding, and MinE stimulation; however, they did eliminate MinD-MinC interaction. Two additional mutations in the switch II region did not affect MinC binding. Further study revealed that one of these allowed the MinCD complex to target to the septum but was still deficient in blocking division. These results indicate that the switch I and II regions of MinD are required for interaction with MinC but not MinE and that the switch II region has a role in activating MinC.

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Membrane Binding by MinD Involves Insertion of Hydrophobic Residues within the C-Terminal Amphipathic Helix into the Bilayer

Cited by 91 publications

References 27 publications

C-Terminal Anchoring of mid1p to Membranes Stabilizes Cytokinetic Ring Position in Early Mitosis in Fission Yeast

C-Terminal Anchoring of mid1p to Membranes Stabilizes Cytokinetic Ring Position in Early Mitosis in Fission Yeast

The Bacterial Cytoskeleton

The Switch I and II Regions of MinD Are Required for Binding and Activating MinC

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