The high-affinity cohesin–dockerin interaction dictates the suprastructural assembly of the multienzyme cellulosome complex. The interaction between these two complementary families of protein modules was found to be species-specific and type-dependent. The structure of the type II cohesin module possesses additional intrinsic secondary structural elements absent in the type I cohesin, i.e., an α-helix and two singular "β-flaps". The role of these extra secondary structures in dockerin recognition was studied in this work using gene swapping, in which corresponding homologous stretches of types I and II cohesins were interchanged. The specificity of binding of the resultant chimaeric cohesins was determined by enzyme-linked affinity assay. Several chimaeric cohesins retained dockerin recognition properties. Hence, these cohesins may undergo manipulations (insertion/deletion of peptide segments) without altering their affinity toward their counterpart dockerin, although type-dependent binding specificity cannot be converted by swapping of the additional secondary structural elements between the two cohesin types. The results further emphasize the strong affinity and plasticity between the cohesin and dockerin pair and are consistent with the known findings on specificity of the types I and II interactions. These studies provide insight into the structural and functional resilience of the cohesins and thus have direct bearing on their potential use in biotechnological applications.
Conference
International Biotechnology Symposium (IBS 2008): "Biotechnology for the Sustainability of Human Society", 13th, Dalian, China, 2008-10-12–2008-10-17
References
1 10.1006/jsbi.1998.4065, E. A. Bayer, L. J. W. Shimon, R. Lamed, Y. Shoham. J. Struct. Biol.124, 221 (1998).Search in Google Scholar
2 R. Lamed, E. Setter, R. Kenig, E. A. Bayer. Biotechnol. Bioeng. Symp.13, 163 (1983).Search in Google Scholar
3 R. Lamed, E. Setter, E. A. Bayer. J. Bacteriol.156, 828 (1983).Search in Google Scholar
4 10.1016/0167-7799(94)90039-6, E. A. Bayer, E. Morag, R. Lamed. Trends Biotechnol.12, 379 (1994).Search in Google Scholar
5 B. Lytle, C. Myers, K. Kruus, J. H. D. Wu. J. Bacteriol.178, 1200 (1996).Search in Google Scholar
6 S. Salamitou, O. Raynaud, M. Lemaire, M. Coughlan, P. Béguin, J.-P. Aubert. J. Bacteriol.176, 2822 (1994).Search in Google Scholar
7 10.1093/protein/6.8.947, K. Tokatlidis, P. Dhurjati, P. Béguin. Protein Eng.6, 947 (1993).Search in Google Scholar
8 10.1016/0014-5793(91)81279-H, K. Tokatlidis, S. Salamitou, P. Béguin, P. Dhurjati, J.-P. Aubert. FEBS Lett.291, 185 (1991).Search in Google Scholar
9 E. Leibovitz, P. Béguin. J. Bacteriol.178, 3077 (1996).Search in Google Scholar
10 E. Leibovitz, H. Ohayon, P. Gounon, P. Béguin. J. Bacteriol.179, 2519 (1997).Search in Google Scholar
11 M. Lemaire, H. Ohayon, P. Gounon, T. Fujino, P. Béguin. J. Bacteriol.177, 2451 (1995).Search in Google Scholar
12 10.1016/S0969-2126(97)00195-0, L. J. W. Shimon, E. A. Bayer, E. Morag, R. Lamed, S. Yaron, Y. Shoham, F. Frolow. Structure5, 381 (1997).Search in Google Scholar
13 10.1006/jmbi.1997.1326, G. A. Tavares, P. Béguin, P. M. Alzari. J. Mol. Biol.273, 701 (1997).Search in Google Scholar PubMed
14 10.1006/jmbi.2000.4191, S. Spinelli, H. P. Fierobe, A. Belaich, J. P. Belaich, B. Henrissat, C. Cambillau. J. Mol. Biol.304, 189 (2000).Search in Google Scholar PubMed
15 10.1016/j.jmb.2005.02.024, I. Noach, F. Frolow, H. Jakoby, S. Rosenheck, L. J. W. Shimon, R. Lamed, E. A. Bayer. J. Mol. Biol.348, 1 (2005).Search in Google Scholar PubMed
16 10.1107/S0907444903014094, I. Noach, R. Lamed, Q. Xu, S. Rosenheck, L. J. W. Shimon, R. Kenig, E. A. Bayer, F. Frolow. Acta Crystallogr., D59, 1670 (2003).Search in Google Scholar
17 10.1016/j.jmb.2005.04.037, A. L. Carvalho, V. M. Pires, T. M. Gloster, J. P. Turkenburg, J. A. Prates, L. M. Ferreira, M. J. Romao, G. J. Davies, C. M. Fontes, H. J. Gilbert. J. Mol. Biol.349, 909 (2005).Search in Google Scholar PubMed
18 10.1074/jbc.M407350200, D. Nakar, T. Handelsman, Y. Shoham, H.-P. Fierobe, J. P. Belaich, E. Morag, R. Lamed, E. A. Bayer. J. Biol. Chem.279, 42881 (2004).Search in Google Scholar PubMed
19 10.1002/jmr.749, Y. Barak, T. Handelsman, D. Nakar, A. Mechaly, R. Lamed, Y. Shoham, E. A. Bayer. J. Mol. Recognit.18, 491 (2005).Search in Google Scholar PubMed
20 10.1093/bioinformatics/btm404, M. A. Larkin, G. Blackshields, N. P. Brown, R. Chenna, P. A. McGettigan, H. McWilliam, F. Valentin, I. M. Wallace, A. Wilm, R. Lopez, J. D. Thompson, T. J. Gibson, D. G. Higgins. Bioinformatics23, 2947 (2007).Search in Google Scholar PubMed
21 10.1093/bioinformatics/btm017, J. Pei, N. V. Grishin. Bioinformatics23, 802 (2007).Search in Google Scholar PubMed
22 E. Morag, A. Lapidot, D. Govorko, R. Lamed, M. Wilchek, E. A. Bayer, Y. Shoham. Appl. Environ. Microbiol.61, 1980 (1995).Search in Google Scholar
23 10.1073/pnas.1936124100, A. L. Carvalho, F. M. Dias, J. A. Prates, T. Nagy, H. J. Gilbert, G. J. Davies, L. M. Ferreira, M. J. Romão, C. M. Fontes. Proc. Natl. Acad. Sci. USA100, 13809 (2003).Search in Google Scholar PubMed PubMed Central
24 10.1073/pnas.0611173104, A. L. Carvalho, F. M. V. Dias, T. Nagy, J. A. M. Prates, M. R. Proctor, N. Smith, E. A. Bayer, G. J. Davies, L. M. A. Ferreira, M. J. Ramão, C. M. G. A. Fontes, H. J. Gilbert. Proc. Natl. Acad. Sci. USA104, 3089 (2007).Search in Google Scholar PubMed PubMed Central
25 10.1074/jbc.M801533200, B. A. Pinheiro, M. R. Proctor, C. C. Martinez-Fleites, J. A. M. Prates, V. A. Money, G. J. Davies, E. A. Bayer, C. M. G. A. Fontes, H.-P. Fierobe, H. J. Gilbert. J. Biol. Chem283, 18422 (2008).Search in Google Scholar PubMed
26 10.1073/pnas.0507109103, J. J. Adams, G. Pal, Z. Jia, S. P. Smith. Proc. Natl. Acad. Sci. USA103, 305 (2006).Search in Google Scholar PubMed PubMed Central
27 E. Gasteiger, C. Hoogland, A. Gattiker, S. Duvaud, M. R. Wilkins, R. D. Appel, A. Bairoch. In The Proteomics Protocols Handbook, J. M. Walker (Ed.), pp. 571–607, Humana Press, Tolowa, NJ (2005).10.1385/1-59259-890-0:571Search in Google Scholar
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