DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. DIP original experiment: DIP-111361X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. DIP original experiment: DIP-111363X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Yura T., Guisbert E., Poritz M., Lu CZ., Campbell E., Gross CA. DIP original experiment: DIP-111362X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. dnaj_ecoli Chaperone protein DnaJ dnaJ groP b0015 Heat shock protein J HSP40 JW0014 protein protein ecoli Escherichia coli (strain K12) MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR DIP protein P08622 original sequence version: 105 DIP protein P08622 original sequence version: 118 DIP protein P08622 original sequence version: 152 DIP protein P08622 original sequence version: null 05FA762EF9844532 rpoh_ecoli RNA polymerase sigma factor RpoH Heat shock regulatory protein F33.4 rpoH fam hin htpR b3461 RNA polymerase sigma-32 factor JW3426 protein protein ecoli Escherichia coli (strain K12) MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA DIP protein P0AGB3 original sequence version: 27 DIP protein P0AGB3 original sequence version: 75 This sequence has been withdrawn from Uniprot. 628A17B4C835D00A ch60_ecoli Chaperonin GroEL groEL 60 kDa chaperonin Chaperonin-60 GroEL protein groL mopA JW4103 b4143 protein protein ecoli Escherichia coli (strain K12) MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM CD3A0FB505F74AD1 CD3A0FB505F74AD1 dnak_ecoli Chaperone protein DnaK dnaK groP grpF seg b0014 Heat shock protein 70 Heat shock 70 kDa protein HSP70 JW0013 protein protein ecoli Escherichia coli (strain K12) MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK DIP protein P0A6Y8 original sequence version: 44 DIP protein P0A6Y8 original sequence version: 96 DIP protein P0A6Y8 original sequence version: 91 DIP protein P0A6Y8 original sequence version: 119 DIP protein P0A6Y8 original sequence version: 95 5A8589B21D7CD9C1 dnaj-rpoh-1 1 4 unspecified role unspecified role bait bait ecolx Escherichia coli 5 unspecified role unspecified role prey prey ecolx Escherichia coli direct interaction direct interaction grol-rpoh-1 3 6 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction dnak-rpoh-1 2 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction