{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:50:13Z","timestamp":1781110213962,"version":"3.54.1"},"reference-count":38,"publisher":"National Academy of Sciences","issue":"19","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,9,12]]},"abstract":"<jats:p>\n                    The cohesin-dockerin interaction in\n                    <jats:italic>Clostridium thermocellum<\/jats:italic>\n                    cellulosome mediates the tight binding of cellulolytic enzymes to the cellulosome-integrating protein CipA. Here, this interaction was used to study the effect of different cellulose-binding domains (CBDs) on the enzymatic activity of\n                    <jats:italic>C. thermocellum<\/jats:italic>\n                    endoglucanase CelD (1,4-\u03b2-\n                    <jats:sc>d<\/jats:sc>\n                    endoglucanase, EC\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"ec\" xlink:href=\"3.2.1.4\">3.2.1.4<\/jats:ext-link>\n                    ) toward various cellulosic substrates. The seventh cohesin domain of CipA was fused to CBDs originating from the\n                    <jats:italic>Trichoderma reesei<\/jats:italic>\n                    cellobiohydrolases I and II (CBD\n                    <jats:sub>CBH1<\/jats:sub>\n                    and CBD\n                    <jats:sub>CBH2<\/jats:sub>\n                    ) (1,4-\u03b2-\n                    <jats:sc>d<\/jats:sc>\n                    glucan-cellobiohydrolase, EC\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"ec\" xlink:href=\"3.2.1.91\">3.2.1.91<\/jats:ext-link>\n                    ), from the\n                    <jats:italic>Cellulomonas fimi<\/jats:italic>\n                    xylanase\/exoglucanase Cex (CBD\n                    <jats:sub>Cex<\/jats:sub>\n                    ) (\u03b2-1,4-\n                    <jats:sc>d<\/jats:sc>\n                    glucanase, EC\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"ec\" xlink:href=\"3.2.1.8\">3.2.1.8<\/jats:ext-link>\n                    ), and from\n                    <jats:italic>C. thermocellum<\/jats:italic>\n                    CipA (CBD\n                    <jats:sub>CipA<\/jats:sub>\n                    ). The CBD-cohesin hybrids interacted with the dockerin domain of CelD, leading to the formation of CelD-CBD complexes. Each of the CBDs increased the fraction of cellulose accessible to hydrolysis by CelD in the order CBD\n                    <jats:sub>CBH1<\/jats:sub>\n                    &lt; CBD\n                    <jats:sub>CBH2<\/jats:sub>\n                    \u2248 CBD\n                    <jats:sub>Cex<\/jats:sub>\n                    &lt; CBD\n                    <jats:sub>CipA<\/jats:sub>\n                    . In all cases, the extent of hydrolysis was limited by the disappearance of sites accessible to CelD. Addition of a batch of fresh cellulose after completion of the reaction resulted in a new burst of activity, proving the reversible binding of the intact complexes despite the apparent binding irreversibility of some CBDs. Furthermore, burst of activity also was observed upon adding new batches of CelD\u2013CBD complexes that contained a CBD differing from the first one. This complementation between different CBDs suggests that the sites made available for hydrolysis by each of the CBDs are at least partially nonoverlapping. The only exception was CBD\n                    <jats:sub>CipA<\/jats:sub>\n                    , whose sites appeared to overlap all of the other sites.\n                  <\/jats:p>","DOI":"10.1073\/pnas.160216697","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:43:20Z","timestamp":1027680200000},"page":"10342-10347","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":225,"title":["Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose"],"prefix":"10.1073","volume":"97","author":[{"given":"G\u00e9raldine","family":"Carrard","sequence":"first","affiliation":[{"name":"VTT Biotechnology, P.O. Box 1500, Espoo FIN-02044, Finland; and Unit\u00e9 de Physiologie Cellulaire and Unit\u00e9 de Recherche Associ\u00e9e 2172 Centre National de la Recherche Scientifique, D\u00e9partement des Biotechnologies, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anu","family":"Koivula","sequence":"additional","affiliation":[{"name":"VTT Biotechnology, P.O. Box 1500, Espoo FIN-02044, Finland; and Unit\u00e9 de Physiologie Cellulaire and Unit\u00e9 de Recherche Associ\u00e9e 2172 Centre National de la Recherche Scientifique, D\u00e9partement des Biotechnologies, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"S\u00f6derlund","sequence":"additional","affiliation":[{"name":"VTT Biotechnology, P.O. Box 1500, Espoo FIN-02044, Finland; and Unit\u00e9 de Physiologie Cellulaire and Unit\u00e9 de Recherche Associ\u00e9e 2172 Centre National de la Recherche Scientifique, D\u00e9partement des Biotechnologies, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre","family":"B\u00e9guin","sequence":"additional","affiliation":[{"name":"VTT Biotechnology, P.O. Box 1500, Espoo FIN-02044, Finland; and Unit\u00e9 de Physiologie Cellulaire and Unit\u00e9 de Recherche Associ\u00e9e 2172 Centre National de la Recherche Scientifique, D\u00e9partement des Biotechnologies, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2000,8,29]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.1994.tb00033.x"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00813506"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2911(08)60143-5"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2690261"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)99167-2"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)36847-4"},{"key":"e_1_3_3_7_2","first-page":"145","volume-title":"Enzymatic Degradation of Insoluble Carbohydrates","author":"Tomme P","year":"1995","unstructured":"P Tomme, A J Warren, R C J Miller, D G Kilburn, N R Gilkes Enzymatic Degradation of Insoluble Carbohydrates, eds J N Saddler, M H Penner (ACS, San Diego) 618, 145\u2013163 (1995)."},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.22.12251"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.38.24016"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.1999.00455.x"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/nbt1191-1096"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.15.4356-4363.1995"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.1993.tb06516.x"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.260420402"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560051117"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1996.tb00960.x"},{"key":"e_1_3_3_17_2","first-page":"45","volume-title":"Genetics, Biochemistry and Ecology of Cellulose Degradation: Mie Bioforum 98","author":"Yaron S","year":"1998","unstructured":"S Yaron, E A Bayer, E Morag, R Lamed, Y Shoham Genetics, Biochemistry and Ecology of Cellulose Degradation: Mie Bioforum 98, eds K Ohmiya, K Hayashi, K Sakka, Y Kobayashi, S Karita, T Kimura (Uni, Suzuka, Japan), pp. 45\u201346 (1998)."},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00444a016"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/8.5.443"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00021a011"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.3109\/10409239609106584"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3260617"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1996.0644"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/9.8.691"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0141-0229(96)00109-3"},{"key":"e_1_3_3_26_2","volume-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook J","year":"1989","unstructured":"J Sambrook, E F Fritsch, T Maniatis Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Lab. 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