{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T01:23:00Z","timestamp":1789521780526,"version":"build-2803163510"},"reference-count":40,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,4,1]]},"abstract":"<jats:p>Chemical arrays were employed to screen ligands for HtpG, the prokaryotic homologue of Hsp (heat-shock protein) 90. We found that colistins and the closely related polymyxin B interact physically with HtpG. They bind to the N-terminal domain of HtpG specifically without affecting its ATPase activity. The interaction caused inhibition of chaperone function of HtpG that suppresses thermal aggregation of substrate proteins. Further studies were performed with one of these cyclic lipopeptide antibiotics, colistin sulfate salt. It inhibited the chaperone function of the N-terminal domain of HtpG. However, it inhibited neither the chaperone function of the middle domain of HtpG nor that of other molecular chaperones such as DnaK, the prokaryotic homologue of Hsp70, and small Hsp. The addition of colistin sulfate salt increased surface hydrophobicity of the N-terminal domain of HtpG and induced oligomerization of HtpG and its N-terminal domain. These structural changes are discussed in relation to the inhibition of the chaperone function.<\/jats:p>","DOI":"10.1042\/bj20100743","type":"journal-article","created":{"date-parts":[[2011,2,17]],"date-time":"2011-02-17T14:24:31Z","timestamp":1297952671000},"page":"237-246","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Cyclic lipopeptide antibiotics bind to the N-terminal domain of the prokaryotic Hsp90 to inhibit the chaperone activity"],"prefix":"10.1042","volume":"435","author":[{"given":"Shun","family":"Minagawa","sequence":"first","affiliation":[{"name":"Molecular Biology Course, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasumitsu","family":"Kondoh","sequence":"additional","affiliation":[{"name":"Chemical Biology Core Facility, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keigo","family":"Sueoka","sequence":"additional","affiliation":[{"name":"Molecular Biology Course, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Osada","sequence":"additional","affiliation":[{"name":"Molecular Biology Course, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan"},{"name":"Chemical Biology Core Facility, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hitoshi","family":"Nakamoto","sequence":"additional","affiliation":[{"name":"Molecular Biology Course, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan"},{"name":"Institute for Environmental Science and Technology (IEST), Saitama University, Saitama 338-8570, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2011,3,15]]},"reference":[{"key":"2021112217382250100_B1","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0092-8674(00)80314-1","article-title":"Identification and structural characterization of the ATP\/ADP-binding site in the Hsp90 molecular chaperone","volume":"90","author":"Prodromou","year":"1997","journal-title":"Cell"},{"key":"2021112217382250100_B2","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1111\/j.1365-2958.2010.07139.x","article-title":"HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942","volume":"76","author":"Sato","year":"2010","journal-title":"Mol. Microbiol."},{"key":"2021112217382250100_B3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1432-1033.1995.001_1.x","article-title":"Mechanism of dimer formation of the 90-kDa heat-shock protein","volume":"233","author":"Nemoto","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"2021112217382250100_B4","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/j.str.2004.03.020","article-title":"The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site","volume":"12","author":"Harris","year":"2004","journal-title":"Structure"},{"key":"2021112217382250100_B5","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1146\/annurev.biochem.75.103004.142738","article-title":"Structure and mechanism of the Hsp90 molecular chaperone machinery","volume":"75","author":"Pearl","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"2021112217382250100_B6","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.cell.2006.09.027","article-title":"Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements","volume":"127","author":"Shiau","year":"2006","journal-title":"Cell"},{"key":"2021112217382250100_B7","doi-asserted-by":"crossref","first-page":"18473","DOI":"10.1074\/jbc.R800007200","article-title":"The Hsp90 chaperone machinery","volume":"283","author":"Wandinger","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021112217382250100_B8","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/358169a0","article-title":"Hsp90 chaperones protein folding in vitro","volume":"358","author":"Wiech","year":"1992","journal-title":"Nature"},{"key":"2021112217382250100_B9","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1038\/35041102","article-title":"Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines","volume":"2","author":"Simizu","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"2021112217382250100_B10","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1177\/153537020322800201","article-title":"Regulation of signaling protein function and trafficking by the hsp90\/hsp70-based chaperone machinery","volume":"228","author":"Pratt","year":"2003","journal-title":"Exp. Biol. Med."},{"key":"2021112217382250100_B11","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.tem.2006.06.003","article-title":"Chaperoning steroid hormone action","volume":"17","author":"Picard","year":"2006","journal-title":"Trends Endocrinol. Metab."},{"key":"2021112217382250100_B12","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.molmed.2004.04.006","article-title":"Therapeutic and diagnostic implications of Hsp90 activation","volume":"10","author":"Kamal","year":"2004","journal-title":"Trends Mol. Med."},{"key":"2021112217382250100_B13","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.2174\/156802606777811979","article-title":"Using natural product inhibitors to validate Hsp90 as a molecular target in cancer","volume":"6","author":"Neckers","year":"2006","journal-title":"Curr. Top. Med. Chem."},{"key":"2021112217382250100_B14","doi-asserted-by":"crossref","first-page":"S7","DOI":"10.1186\/1471-2202-9-S2-S7","article-title":"Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?","volume":"9","author":"Luo","year":"2008","journal-title":"BMC Neurosci."},{"key":"2021112217382250100_B15","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1038\/nm1298","article-title":"17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration","volume":"11","author":"Waza","year":"2005","journal-title":"Nat. Med."},{"key":"2021112217382250100_B16","doi-asserted-by":"crossref","first-page":"7967","DOI":"10.1021\/ja991083q","article-title":"Printing small molecules as microarrays and detecting protein? Ligand interactions en masse","volume":"121","author":"MacBeath","year":"1999","journal-title":"J. Am. Chem. Soc."},{"key":"2021112217382250100_B17","doi-asserted-by":"crossref","first-page":"5584","DOI":"10.1002\/anie.200352164","article-title":"Immobilization of natural products on glass slides by using a photoaffinity reaction and the detection of protein\u2013small-molecule interactions","volume":"42","author":"Kanoh","year":"2003","journal-title":"Angew. Chem. Int. Ed."},{"key":"2021112217382250100_B18","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1002\/asia.200600208","article-title":"Photo-cross-linked small-molecule microarrays as chemical genomic tools for dissecting protein\u2013ligand interactions","volume":"1","author":"Kanoh","year":"2006","journal-title":"Chem. Asian J."},{"key":"2021112217382250100_B19","doi-asserted-by":"crossref","first-page":"2739","DOI":"10.1271\/bbb.80383","article-title":"Robust and systematic drug screening method using chemical arrays and the protein library: identification of novel inhibitors of carbonic anhydrase II","volume":"72","author":"Miyazaki","year":"2008","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"2021112217382250100_B20","doi-asserted-by":"crossref","first-page":"4398","DOI":"10.1016\/S0021-9258(18)83755-3","article-title":"Purification and properties of the Escherichia coli heat shock protein, HtpG","volume":"264","author":"Spence","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2021112217382250100_B21","doi-asserted-by":"crossref","first-page":"14412","DOI":"10.1074\/jbc.270.24.14412","article-title":"Structural organization of procaryotic and eucaryotic Hsp90: influence of divalent cations on structure and function","volume":"270","author":"Jakob","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021112217382250100_B22","first-page":"3919","article-title":"hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures","volume":"9","author":"Borkovich","year":"1989","journal-title":"Mol. Cell. Biol."},{"key":"2021112217382250100_B23","doi-asserted-by":"crossref","first-page":"2977","DOI":"10.1128\/jb.170.7.2977-2983.1988","article-title":"Ancient heat shock gene is dispensable","volume":"170","author":"Bardwell","year":"1988","journal-title":"J. Bacteriol."},{"key":"2021112217382250100_B24","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0378-1119(96)00317-4","article-title":"Cloning and characterization of the Actinobacillus actinomycetemcomitans gene encoding a heat-shock protein 90 homologue","volume":"179","author":"Winston","year":"1996","journal-title":"Gene"},{"key":"2021112217382250100_B25","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1007\/s004380051004","article-title":"The Bacillus subtilis htpG gene is not involved in thermal stress management","volume":"261","author":"Versteeg","year":"1999","journal-title":"Mol. Gen. Genet."},{"key":"2021112217382250100_B26","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0014-5793(99)01134-5","article-title":"HtpG is essential for the thermal stress management in cyanobacteria","volume":"458","author":"Tanaka","year":"1999","journal-title":"FEBS Lett."},{"key":"2021112217382250100_B27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0021-9258(17)31212-7","article-title":"Light guides: directional energy transfer in a photosynthetic antenna","volume":"264","author":"Glazer","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2021112217382250100_B28","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1128\/mr.57.3.725-749.1993","article-title":"The phycobilisome, a light-harvesting complex responsive to environmental conditions","volume":"57","author":"Grossman","year":"1993","journal-title":"Microbiol. Rev."},{"key":"2021112217382250100_B29","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1128\/CMR.00006-08","article-title":"Polymyxins revisited","volume":"21","author":"Landman","year":"2008","journal-title":"Clin. Microbiol. Rev."},{"key":"2021112217382250100_B30","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1086\/429323","article-title":"Colistin: the revival of polymyxins for the management of multidrug-resistant Gram-negative bacterial infections","volume":"40","author":"Falagas","year":"2005","journal-title":"Clin. Infect. Dis."},{"key":"2021112217382250100_B31","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1128\/AAC.47.4.1364-1370.2003","article-title":"Stability of colistin and colistin methanesulfonate in aqueous media and plasma as determined by high-performance liquid chromatography","volume":"47","author":"Li","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112217382250100_B32","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1128\/JB.183.4.1320-1328.2001","article-title":"Characterization of the dnaK multigene family in the cyanobacterium Synechococcus sp. strain PCC7942","volume":"183","author":"Nimura","year":"2001","journal-title":"J. Bacteriol."},{"key":"2021112217382250100_B33","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1021\/ac051777j","article-title":"SPR imaging of photo-cross-linked small-molecule arrays on gold","volume":"78","author":"Kanoh","year":"2006","journal-title":"Anal. Chem."},{"key":"2021112217382250100_B34","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1002\/asia.200800099","article-title":"Improvement of photoaffinity SPR imaging platform and determination of the binding site of p62\/SQSTM1 to p38 MAP kinase","volume":"3","author":"Saito","year":"2008","journal-title":"Chem. Asian J."},{"key":"2021112217382250100_B35","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1271\/bbb.100493","article-title":"Comparative biochemical characterization of two GroEL homologs from the cyanobacterium Synechococcus elongatus PCC 7942","volume":"74","author":"Huq","year":"2010","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"2021112217382250100_B36","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0014-5793(97)01363-X","article-title":"In vitro evidence that hsp90 contains two independent chaperone sites","volume":"418","author":"Young","year":"1997","journal-title":"FEBS Lett."},{"key":"2021112217382250100_B37","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1007\/s00018-006-6321-2","article-title":"The small heat shock proteins and their clients","volume":"64","author":"Nakamoto","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"key":"2021112217382250100_B38","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1042\/bj2820589","article-title":"Spectrofluorimetric assessment of the surface hydrophobicity of proteins","volume":"282","author":"Cardamone","year":"1992","journal-title":"Biochem. J."},{"key":"2021112217382250100_B39","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1074\/jbc.271.5.2641","article-title":"Heat-induced chaperone activity of HSP90","volume":"271","author":"Yonehara","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021112217382250100_B40","doi-asserted-by":"crossref","first-page":"4133","DOI":"10.1074\/jbc.274.7.4133","article-title":"Heat-induced oligomerization of the molecular chaperone Hsp90: inhibition by ATP and geldanamycin and activation by transition metal oxyanions","volume":"274","author":"Chadli","year":"1999","journal-title":"J. Biol. Chem."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/435\/1\/237\/667667\/bj4350237.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/435\/1\/237\/667667\/bj4350237.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T01:47:58Z","timestamp":1637632078000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/435\/1\/237\/88464\/Cyclic-lipopeptide-antibiotics-bind-to-the-N"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,3,15]]},"references-count":40,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2011,4,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20100743","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,3,15]]}}}