IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding. Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2001 imex curation Torok Z., Goloubinoff P., Horvath I., Tsvetkova NM., Glatz A., Balogh G., Varvasovszki V., Los DA., Vierling E., Crowe JH., Vigh L. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The comigration in gel is run at 47 degres under non denaturing conditions to test the ability of HSP17 to bind heat-denaturing proteins. Fig. 1 vigh@nucleus.szbk.u-szeged.hu Only protein-protein interactions in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel western blot western blot Immuno blot Immuno blot Torok Z., Goloubinoff P., Horvath I., Tsvetkova NM., Glatz A., Balogh G., Varvasovszki V., Los DA., Vierling E., Crowe JH., Vigh L. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The comigration in gel is run at 47 degres under non denaturing conditions to test the ability of HSP17 to bind heat-denaturing proteins. Fig. 1 vigh@nucleus.szbk.u-szeged.hu Accepted 2006-MAR-21 by KROBBE. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2001 Only protein-protein interactions imex curation mdhm_pig Malate dehydrogenase, mitochondrial MDH2 protein protein pig Sus scrofa (Pig) Pig MLSALARPAGAALRRSFSTSXQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAELKGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLSTLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLGIGKISPFEEKMIAEAIPELKASIKKGEEFVKNMK B0435E87383D0B1E p72977_syny3 hsp17 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSLILYNPLREMDNFQQQMNQLFEEVFVPTDRHGDRQGFNPKAELTETEEAYVLKLELPGMDPDNLDIQAARDAVTVSGDRQDTHSTEKDGVRRTEFRYGSFRRVIPVPGAIQNTEVKANYDAGILTLTLPKVEEAKNKVVKVQLS 4453B15DF8F9EABE hsp17-mdh-1 1 2 unspecified role unspecified role neutral component neutral component pig Sus scrofa (Pig) Pig 3 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction HSP17 assists the complete refolding of heat denaturated MDH in presence of E. coli DnaK, DnaJ, GrpE, GroEL, GroES (see fig.2). P72977 purified P00346 purified In contrast, when HSP17 was incubated at 47�C in the presence of increasing amounts of denaturing MDH, the two proteins formed increasing and saturating amounts of gel-electrophoresis-resistant oligomers, which were larger than 800 kDa at the expense of the initial low molecular mass species (Fig. 1).