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 Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. EMBO J. (0261-4189) 2011 imex curation Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. EMBO J. (0261-4189) 2011 imex curation Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. EMBO J. (0261-4189) 2011 imex curation Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. Only protein-protein interactions ecoli Escherichia coli (strain K12) 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. Conjugal plasmid transfer in Streptomyces resembles bacterial chromosome segregation by FtsK/SpoIIIE. EMBO J. (0261-4189) 2011 imex curation Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Vogelmann J., Ammelburg M., Finger C., Guezguez J., Linke D., Flötenmeyer M., Stierhof YD., Wohlleben W., Muth G. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation q3laj2_strvz traB protein protein strvz Streptomyces venezuelae MTEHLTEKNPAPADFDSIATVTFLRPTLPAPASVPEDNTWSDMPDDTDPAVVIPPMPTVAPAIGSDERTVVLETARVILDKTPAVEPVVRPGRFAGTVDLDDFDDAPLIPAWMYSAEGWAAWAGVFYRARRRDFRRWVRRQPTQHGHVRQFGRGTRRAHEWVVGFEGVRVQSAAHTAHVLTREARLAARHARFTPRILGSKKELAMKAADKATKAAEEAVLLHKKAKKDRNRVRNLRAGVVYGPPLTAIGTGYVMGGGLGLAAGLLSTFAGGAFVGRKPYDEEADWTSDWRSLGDGDRMTAPMLDASFRAAKVIGAEETLGVVQMPMLDTRGAWTAVLDLPPGVPAKKAIRATDELAAAFGVEEAQVSVAKRGRAGRIELYVARELPFTDKAAPGPLLALESAADFWGRISIGPDVRGIHQSISVVERSGLIGGEPGAGKSASGNTILLAAALDPRVILWLADGKGGGDLEPFEHLCERYEGDADPEAFNAMLDELLDVMKARYALLKKLGKRKVTEELANKYPELRQLLLWVDELMLYTTAEEFGKKITRKLRNLVSRGRAAGIITFCATQKPGSDVVDTSLRDLLSIRWALRCTTPEASDTILGKGAAASGYSAKTIQSEMRGAGLLWAEGTNPTMVRADYYDDDQVTALIERATEWRRKAGTLPNGPVPLVDQLRARGDDDALLLAAVLEVFAAQATEDDPVDWLPGQLLVDELKAAGHSVTAEKLGALVVRTDEEKAKRPWGEKKTRVTGYPLARVEAAATDRFGLTA mint F51308F34FF661CC trab-1 2 traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 6.0 direct interaction direct interaction mint Using electron microscopy we detected ring-shaped hexameric structures of TraB resembling those of the DNA-translocase domain of Pseudomonas aeruginosa FtsK (Massey et al, 2006). Interestingly, soluble TraBs lacking the N-terminal 270 aa membrane-anchor region (Figure 6B) produced similar hexameric complexes as full-length TraB (Figure 6C). f6b f6c f6d f6e sf8 trab-1 4 traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 6.0 direct interaction direct interaction f6a mint Analytical gel filtration of TraBs suggested a hexameric conformation (Figure 6A) trab-trab-8 1 traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf6 mint Chemical crosslinking of TraBs showed high molecular weight TraB complexes, and thus oligomerization (Supplementary Figure S6). trab-trab-9 3 traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell tandem tag tandem tag tandem tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain traB 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association mint sf7 In bacterial two-hybrid analyses (Karimova et al, 1998), we obtained evidence that both the N-terminal 130 aa and the C-terminal wHTH domain of TraB are involved in oligomerization (Supplementary Figure S7).