Structural analysis of the interaction between the bacterial cell division proteins FtsQ and FtsB

Kureisaite-Ciziene, Danguole; Varadajan, Aravindan; McLaughlin, Stephen H.; Glas, Marjolein; Silva, Alejandro Montón; Luirink, Rosa A.; Mueller, Carolin; Blaauwen, Tanneke den; Grossmann, Tom N.; Luirink, Joen; Löwe, Jan

doi:10.1101/362335

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“…Exactly how and in what stoichiometry the complex forms and functions is still a matter of debate 19,22–25 . Interactions between FtsB and FtsL seem to rely on their coiled-coil transmembrane helices 19,24 while the interaction of FtsQ and FtsB requires their periplasmic soluble domains and forms independently of FtsL 23,26,27 . Our findings seem to confirm the former interaction in vivo and provide a tool for the further dissection of FtsQLB interactions.…”

Section: Discussionmentioning

confidence: 99%

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

Meiresonne

Consoli

Mertens

et al. 2018

Preprint

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1 the bacterial periplasm allows high 2 efficiency in vivo FRET of cell division 3 antibiotic targets. Abstract 8 Fluorescent proteins (FP)s are of vital importance to biomedical research. Many of the currently 9available fluorescent proteins do not fluoresce when expressed in non-native environments, such as 10 the bacterial periplasm. This strongly limits the options for applications that employ multiple FPs, such 11 as multiplex imaging or FRET. To address this issue, we have engineered a new cyan fluorescent protein 12 based on mTurquoise2 (mTq2). The new variant is dubbed superfolder turquoise 2 ox (sfTq2 ox ) and is 13 able to withstand challenging, oxidizing environments. sfTq2 ox has improved folding capabilities and 14 can be expressed in the periplasm at higher concentrations without toxicity. This was tied to the 15 replacement of native cysteines that may otherwise form promiscuous disulfide-bonds. The improved 16 sfTq2 ox has the same spectroscopic properties as mTq2, i.e. high fluorescence lifetime and quantum 17 yield. The sfTq2 ox -mNeongreen FRET pair allows the detection of periplasmic protein-protein 18 interactions with energy transfer rates exceeding 40 %. Employing the new FRET pair, we show the 19 direct interaction of two essential periplasmic cell division proteins FtsL and FtsB and disrupt it by 20 mutations, paving the way for in vivo antibiotic screening. 21 22

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Section: Discussionmentioning

confidence: 99%

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

Meiresonne

Consoli

Mertens

et al. 2018

Preprint

View full text Add to dashboard Cite

show abstract

Structural analysis of the interaction between the bacterial cell division proteins FtsQ and FtsB

Cited by 1 publication

References 43 publications

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

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Structural analysis of the interaction between the bacterial cell division proteins FtsQ and FtsB

Cited by 1 publication

References 43 publications

Superfolder mTurquoise2oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

Superfolder mTurquoise2oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

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Product

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About

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets

Superfolder mTurquoise2^oxoptimized for the bacterial periplasm allows high efficiencyin vivoFRET of cell division antibiotic targets