MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. FEBS Lett. (0014-5793) 2015 imex curation Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu Accepted 2015-FEB-13 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. FEBS Lett. (0014-5793) 2015 imex curation Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati weight by comassie molecular weight estimation by coomasie staining weight by comassie Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu Accepted 2015-FEB-13 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. FEBS Lett. (0014-5793) 2015 imex curation Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu Accepted 2015-FEB-13 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide. FEBS Lett. (0014-5793) 2015 imex curation Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Conti J., Viola M.G., Camberg J.L. cambergj@mail.uri.edu Accepted 2015-FEB-13 by LUANA FEBS Lett. (0014-5793) 2015 Only protein-protein interactions imex curation mind_ecoli Septum site-determining protein MinD Cell division inhibitor MinD minD b1175 JW1164 protein protein ecoli Escherichia coli (strain K12) MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG DIP protein P0AEZ3 original sequence version: 74 DIP protein P0AEZ3 original sequence version: 39 0D2C4C0976B77D2C minc_ecoli Septum site-determining protein MinC minC b1176 JW1165 protein protein ecoli Escherichia coli (strain K12) MSNTPIELKGSSFTLSVVHLHEAEPKVIHQALEDKIAQAPAFLKHAPVVLNVSALEDPVNWSAMHKAVSATGLRVIGVSGCKDAQLKAEIEKMGLPILTEGKEKAPRPAPTPQAPAQNTTPVTKTRLIDTPVRSGQRIYAPQCDLIVTSHVSAGAELIADGNIHVYGMMRGRALAGASGDRETQIFCTNLMAELVSIAGEYWLSDQIPAEFYGKAARLQLVENALTVQPLN DIP protein P18196 original sequence version: 116 DIP protein P18196 original sequence version: 82 DIP protein P18196 original sequence version: null E4283A6AD850DAD0 minc-mind-5 2 5 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified 6 weight by comassie molecular weight estimation by coomasie staining weight by comassie weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1a f2a sf1a sf1d MinC and MinD were incubated in the presence and absence of ATP, and then reactions were fractionated by ultracentrifugation. We observed that without ATP, both MinD and MinC, alone or together, were soluble and predominantly localized to the supernatant (Fig. 1A). However, when MinC and MinD were incubated together with ATP, the distribution of both proteins shifted to the pellet even though only MinD contains a nucleotide- binding site (46% of MinD fractionated with the pellet). The ratio of MinD to MinC was calculated to be 1.6:1 (Fig. S1A). minc-mind-6 4 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2b f2c f2d f5 MinE disassembles ATP-dependent MinCD polymers. minc-mind-7 3 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1b sf1b MinE disassembles ATP-dependent MinCD polymers. minc-mind-8 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3