Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 73–76 | Cite as

Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824



Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond these groups and emanate from a branching point between the type I and type III cohesins. Cohesins and dockerins from C. acetobutylicum show low sequence homology to those from other cellulolytic bacteria, and their interactions are specific in corresponding species. Therefore the interactions between cohesins and dockerins from C. acetobutylicum are meaningful to the studies of both cellulosome assembling mechanism and the construction of designer cellulosome. Here we report the NMR resonance assignments of one cohesin from cellulosome scaffoldin cipA and one dockerin from a cellulosomal glycoside hydrolase (family 9) of C. acetobutylicum for further structural determination and functional studies.


Cohesin Dockerin Clostridium acetobutylicum Cellulosome NMR 



This work was supported by One-Hundred-Talented-People program (KSCX2-YW-G-066) from Chinese Academy of Sciences, the National Basic Research Program of China (973 Program, Grant No. 2011CB707404), and the National Natural Science Foundation of China (Grant No. 31100568).


  1. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) Nmrpipe—a multidimensional spectral processing system based on Unix pipes. J Biomol NMR 6(3):277–293. doi: 10.1007/BF00197809 CrossRefGoogle Scholar
  2. Fontes CMGA, Gilbert HJ (2010) Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. Annu Rev Biochem 79:655–681. doi: 10.1146/annurev-biochem-091208-085603 CrossRefGoogle Scholar
  3. Haimovitz R, Barak Y, Morag E, Voronov-Goldman M, Shoham Y, Lamed R, Bayer EA (2008) Cohesin–dockerin microarray: diverse specificities between two complementary families of interacting protein modules. Proteomics 8(5):968–979. doi: 10.1002/pmic.200700486 CrossRefGoogle Scholar
  4. Johnson BA, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4(5):603–614. doi: 10.1007/BF00404272 CrossRefGoogle Scholar
  5. Maki M, Leung KT, Qin WS (2009) The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass. Int J Biol Sci 5(5):500–516CrossRefGoogle Scholar
  6. Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wuthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids—(IUPAC Recommendations. Pure Appl Chem 70(1):117–142. doi: 10.1351/pac199870010117 CrossRefGoogle Scholar
  7. Mingardon F, Perret S, Belaich A, Tardif C, Belaich JP, Fierobe HP (2005) Heterologous production, assembly, and secretion of a minicellulosome by Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol 71(3):1215–1222. doi: 10.1128/Aem.71.3.1215-1222.2005 CrossRefGoogle Scholar
  8. Sabathe F, Soucaille P (2003) Characterization of the CipA scaffolding protein and in vivo production of a mini cellulosome in Clostridium acetobutylicum. J Bacteriol 185(3):1092–1096. doi: 10.1128/Jb.185.3.1092-1096.2003 CrossRefGoogle Scholar
  9. Sabathe F, Belaich A, Soucaille P (2002) Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum. FEMS Microbiol Lett 217(1):15–22. doi: 10.1111/j.1574-6968.2002.tb11450.x CrossRefGoogle Scholar
  10. Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213–223. doi: 10.1007/s10858-009-9333-z CrossRefGoogle Scholar

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© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  1. 1.Qingdao Institute of Bioenergy and Bioprocess TechnologyChinese Academy of SciencesQingdaoChina

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