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Chaperones tested include \u03b1\u2010crystallin from bovine eye lenses, HSP16.3, HSP70 from <jats:italic>Mycobacterium tuberculosis<\/jats:italic> and \u03b1 <jats:sub>s<\/jats:sub>\u2010casein from milk. All of them inhibit polymerization in a dose\u2010dependent manner independent of assembly inducers used. The critical concentration of MTP polymerization increases with increasing concentration of HSP16.3. Increase in chaperone concentration lowers the extent of polymerization and increases the lag time of self\u2010assembly reaction. Although the addition of a chaperone at the early stage of elongation phase shows no effect on polymerization, the same concentration of chaperone inhibits polymerization completely when added before the initiation of polymerization. Bindings of HSP16.3 and \u03b1 <jats:sub>s<\/jats:sub>\u2010casein to tubulin have been confirmed using isothermal titration calorimetry. Affinity constants of tubulin are 5.3 \u00d7\u00d7 10<jats:sup>4<\/jats:sup> and 9.8 \u00d7\u00d7 10<jats:sup>5<\/jats:sup> M<jats:sup>\u22121<\/jats:sup> for HSP16.3 and \u03b1 <jats:sub>s<\/jats:sub>\u2010casein, respectively. Thermodynamic parameters indicate favourable entropy and enthalpy changes for both chaperones\u2010tubulin interactions. Positive entropy change suggests that the interaction is hydrophobic in nature and desolvation occurring during formation of tubulin\u2010chaperone complex. On the basis of thermodynamic data and observations made upon addition of chaperone at early elongation phase or before the initiation of polymerization, we hypothesize that chaperones bind tubulin at the protein\u2010protein interaction site involved in the nucleation phase of self\u2010assembly. Proteins 2007. \u00a9 2007 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.21286","type":"journal-article","created":{"date-parts":[[2007,1,22]],"date-time":"2007-01-22T23:47:54Z","timestamp":1169509674000},"page":"112-120","source":"Crossref","is-referenced-by-count":9,"title":["Chaperone\u2010mediated inhibition of tubulin self\u2010assembly"],"prefix":"10.1002","volume":"67","author":[{"given":"Gopa","family":"Mitra","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Abhik","family":"Saha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Twishasri Das","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Asim","family":"Poddar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kali P.","family":"Das","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sujoy K.","family":"Das Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bhabatarak","family":"Bhattacharyya","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2007,1,22]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.bjc.6600960"},{"key":"e_1_2_7_3_2","first-page":"1214","article-title":"Dicoumarol: a unique microtubule stabilizing natural product that is synergistic with Taxol","volume":"63","author":"Madari H","year":"2003","journal-title":"Cancer Res"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi992217f"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.20.10560"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0955-0674(99)00056-3"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0169(1996)35:1<24::AID-CM2>3.0.CO;2-I"},{"key":"e_1_2_7_8_2","first-page":"1177","article-title":"Low potency of taxol at microtubule minus ends: implications for its antimitotic and therapeutic mechanism","volume":"58","author":"Derry WB","year":"1998","journal-title":"Cancer Res"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1247\/csf.24.329"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1247\/csf.24.345"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20031413"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0369-8114(02)00324-3"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E03-03-0126"},{"key":"e_1_2_7_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/39382"},{"key":"e_1_2_7_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00684a032"},{"key":"e_1_2_7_16_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF02918353"},{"key":"e_1_2_7_17_2","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1093\/oxfordjournals.jbchem.a134955","article-title":"33K protein\u2014an inhibitory factor of tubulin polymerization in porcine brain","volume":"96","author":"Kotani S","year":"1984","journal-title":"J Biochem (Tokyo)"},{"key":"e_1_2_7_18_2","doi-asserted-by":"crossref","first-page":"6306","DOI":"10.1016\/S0021-9258(20)65140-7","article-title":"Two opposing effects of calmodulin on microtubule assembly depend on the presence of microtubule\u2010associated proteins","volume":"257","author":"Lee YC","year":"1982","journal-title":"J Biol Chem"},{"key":"e_1_2_7_19_2","doi-asserted-by":"crossref","first-page":"11216","DOI":"10.1016\/S0021-9258(19)68580-7","article-title":"Intrinsic calcium sensitivity of tubulin polymerization. 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