Fluorescence Polarization Analysis for Revealing Molecular Mechanism of Nucleotide-Dependent Phospholipid Membrane Binding of MinD Adenosine 5'-Triphosphate, Adenosine Triphosphatase

Okuno, Takashi; Ohgita, Takashi; Sasa, Tatsunori; Nonaka, Aoi; Funasaki, Noriaki; Kogure, Kentaro

doi:10.1248/bpb.33.1746

Cited by 4 publications

(4 citation statements)

References 26 publications

(12 reference statements)

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“…The sedimentation of DNA was strongly reduced in the presence of mutant MinD R219D (Figure 2G). Interestingly, substantial sedimentation of DNA was observed for MinD K11A mutant that is not able to dimerize (Zhou et al , 2005) but is still able to bind ATP (Okuno et al , 2010), indicating that binding of multiple monomers to the same DNA fragment may be sufficient to form HMW nucleoprotein complexes. MinD K11A –DNA complexes were also detected in EMSAs (Supplementary Figure S2B).…”

Section: Resultsmentioning

confidence: 99%

Chromosome segregation by the Escherichia coli Min system

Ventura

Knecht

Andreas

et al. 2013

Molecular Systems Biology

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Section: Resultsmentioning

confidence: 99%

Chromosome segregation by the Escherichia coli Min system

Ventura

Knecht

Andreas

et al. 2013

Molecular Systems Biology

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“…The mutant protein MinD(K11A) is unable to dimerize or polymerize with MinC, yet is reported to bind ATP (Fig. 6B) [34]. Deletion of the MTS from MinD prevents polymerization with MinC ( Fig.…”

Section: Discussionmentioning

confidence: 98%

“…6A) [21,22]. However, MinD(K11A) binds nucleotide with similar affinity as wild type MinD [34]. The cooperativity observed with wild type MinD suggests that oligomerization is likely important for polymerization with MinC.…”

Section: Mutations In Mind Prevent Polymerization With Mincmentioning

confidence: 95%

The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

2014

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Edited by Renee TsolisKeywords: MinE ATPase Phospholipids Cytokinesis Min system a b s t r a c tThe Min system of proteins, consisting of MinC, MinD and MinE, is essential for normal cell division in Escherichia coli. MinC forms a polar gradient to restrict placement of the division septum to midcell. MinC localization occurs through a direct interaction with MinD, a membrane-associating Par-like ATPase. MinE stimulates ATP hydrolysis by MinD, thereby releasing MinD from the membrane. Here, we show that MinD forms polymers with MinC and ATP without the addition of phospholipids. The topological regulator MinE induces disassembly of MinCD polymers. Two MinD mutant proteins, MinD(K11A) and MinD(DMTS 15 ), are unable to form polymers with MinC.

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“…The ttMutS mutant derivatives K597M and E671A showed k cat values 5-and 18-fold smaller than WT, respectively (Table 1). It is known that the conserved lysine and glutamate residues in Walker A and B motifs are crucial for the ATPase activity; however, it is also reported that mutagenizing these residues to others results in only partial abolishment of the ATPase activity [51][52][53]. The K m value of the K597M mutant was similar to that of WT and was sufficiently smaller than the ATP concentration (750 lM) used for the endonuclease assay.…”

Section: Activation Of Ttmutl Required Atp Hydrolysis By Ttmutsmentioning

confidence: 89%

MutS stimulates the endonuclease activity of MutL in an ATP‐hydrolysis‐dependent manner

et al. 2013

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In the initial steps of DNA mismatch repair, MutS recognizes a mismatched base and recruits the latent endonuclease MutL onto the mismatch-containing DNA in concert with other proteins. MutL then cleaves the error-containing strand to introduce an entry point for the downstream excision reaction. Because MutL has no intrinsic ability to recognize a mismatch and discriminate between newly synthesized and template strands, the endonuclease activity of MutL is strictly regulated by ATP-binding in order to avoid nonspecific degradation of the genomic DNA. However, the activation mechanism for its endonuclease activity remains unclear. In this study, we found that the coexistence of a mismatch, ATP and MutS unlocks the ATP-binding-dependent suppression of MutL endonuclease activity. Interestingly, ATPase-deficient mutants of MutS were unable to activate MutL. Furthermore, wild-type MutS activated ATPase-deficient mutants of MutL less efficiently than wild-type MutL. We concluded that ATP hydrolysis by MutS and MutL is involved in the mismatch-dependent activation of MutL endonuclease activity.

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Fluorescence Polarization Analysis for Revealing Molecular Mechanism of Nucleotide-Dependent Phospholipid Membrane Binding of MinD Adenosine 5'-Triphosphate, Adenosine Triphosphatase

Cited by 4 publications

References 26 publications

Chromosome segregation by the Escherichia coli Min system

Chromosome segregation by the Escherichia coli Min system

The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

MutS stimulates the endonuclease activity of MutL in an ATP‐hydrolysis‐dependent manner

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