FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in
            <i>Escherichia coli</i>

Guzman, Luz-Maria; Barondess, James J.; Beckwith, Jon

doi:10.1128/jb.174.23.7717.1992

Cited by 143 publications

(155 citation statements)

References 45 publications

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“…N-terminal sequencing yielded the sequence VKEYDIVA. Combining the mass and sequence data indicated that the fragment spans residues 220 to 361 of pneumococcal DivIB (15,843 Da). This fragment overlaps the ␤-domain defined by the structure of FtsQ from E. coli, and is somewhat longer on the C-terminal side than the ␤-domain defined by partial proteolysis of DivIB from G. stearothermophilus.…”

Section: Resultsmentioning

confidence: 99%

“…Both ␤ and ␤␥ contain an additional N-terminal glycine resulting from cleavage of the fusion with the GST using the TEV protease. 15 N atoms, i.e. the amide protons of the backbone chain and the few amine protons from side chains.…”

Section: Resultsmentioning

confidence: 99%

“…The TEV protease was then removed by binding on Ni-NTA resin (Qiagen). This procedure was sufficient for the 15 Further purification steps were also applied before scattering experiments. DivIB ext , ␤, and ␤␥ proteins from the affinity purification were dialyzed against 20 mM Tris, pH 8, to lower the NaCl concentration to 15 mM, prior to loading onto a Resource Q resin (GE Healthcare) and elution with a NaCl gradient from 15 to 500 mM in 10 column volumes.…”

Section: Methodsmentioning

confidence: 99%

“…When an excess of unlabeled (KL/EC) was added to 15 NDivIB ext , at a concentration where most of the DivIB ext should be interacting with the dimer, the [ 15 N-1 H]HSQC spectrum showed the disappearance of nearly all the dispersed peaks and the persistence of the peaks due to unfolded parts of the protein (not shown). We interpreted these observations as indicating that the (KL/EC) dimer interacts with the ␤-domain of DivIB, without important contact with the ␣-or ␥-regions.…”

Section: Nmr Investigations Of the Extracellular Part Of Divib And Itmentioning

confidence: 99%

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Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod

Masson

Kern

Gouëllec

et al. 2009

Journal of Biological Chemistry

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DivIB(FtsQ), FtsL, and DivIC(FtsB) are enigmatic membrane proteins that are central to the process of bacterial cell division. DivIB(FtsQ) is dispensable in specific conditions in some species, and appears to be absent in other bacterial species. The presence of FtsL and DivIC(FtsB) appears to be conserved despite very low sequence conservation. The three proteins form a complex at the division site, FtsL and DivIC(FtsB) being associated through their extracellular coiled-coil region. We report here structural investigations by NMR, small-angle neutron and x-ray scattering, and interaction studies by surface plasmon resonance, of the complex of DivIB, FtsL, and DivIC from Streptococcus pneumoniae, using soluble truncated forms of the proteins. We found that one side of the "bean"-shaped central ␤-domain of DivIB interacts with the C-terminal regions of the dimer of FtsL and DivIC. This finding is corroborated by sequence comparisons across bacterial genomes. Indeed, DivIB is absent from species with shorter FtsL and DivIC proteins that have an extracellular domain consisting only of the coiled-coil segment without C-terminal conserved regions (Campylobacterales). We propose that the main role of the interaction of DivIB with FtsL and DivIC is to help the formation, or to stabilize, the coiled-coil of the latter proteins. The coiled-coil of FtsL and DivIC, itself or with transmembrane regions, could be free to interact with other partners.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Nmr Investigations Of the Extracellular Part Of Divib And Itmentioning

confidence: 99%

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Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod

Masson

Kern

Gouëllec

et al. 2009

Journal of Biological Chemistry

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“…Cells were grown routinely in NZY medium (15). For testing growth on minimal medium M63 was used as described (14).…”

Section: Methodsmentioning

confidence: 99%

Thioredoxin 2 Is Involved in the Oxidative Stress Response inEscherichia coli

Ritz¹,

Patel²,

Doan³

et al. 2000

Journal of Biological Chemistry

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141

123

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Two genes encoding thioredoxin are found on the Escherichia coli genome. Both of them are capable of reducing protein disulfide bonds in vivo and in vitro. The catalytic site contains a Cys-X 1 -X 2 -Cys motif in a so-called thioredoxin fold. Thioredoxin 2 has two additional pairs of cysteines in a non-conserved N-terminal domain. This domain does not appear to be important for the function of thioredoxin 2 in donating electrons to ribonucleotide reductase, 3-phosphoadenylsulfate-reductase, or the periplasmic disulfide isomerase DsbC. Our results suggests that the two thioredoxins are equivalent for most of the in vivo functions that were tested. On the other hand, transcriptional regulation is different. The expression of trxC is regulated by the transcriptional activator OxyR in response to oxidative stress. Oxidized OxyR binds directly to the trxC promoter and induces its expression in response to elevated hydrogen peroxide levels or the disruption of one or several of the cytoplasmic redox pathways. Mutants lacking thioredoxins 1 and 2 are more resistant to high levels of hydrogen peroxide, whereas they are more sensitive to diamide, a disulfide bond-inducing agent.

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In-cell Nuclear Magnetic Resonance Spectroscopy

Burz

Shekhtman

2011

Encyclopedia of Magnetic Resonance

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FtsL, an Essential Cytoplasmic Membrane Protein Involved in Cell Division in Escherichia coli

Cited by 143 publications

References 45 publications

Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod

Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod

Thioredoxin 2 Is Involved in the Oxidative Stress Response inEscherichia coli

In-cell Nuclear Magnetic Resonance Spectroscopy

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