Abstract
The cellulosome of Clostridium thermocellum is an elegant and efficient multi-enzyme complex for degrading lignocellulose. The cellulosome contains several dozens of carbohydrate hydrolysis enzymes, which are regulated by the presence of environmental substrates through several pairs of sigma and anti-sigma factors. The anti-sigma factors sense the presence of substrates and transduce the signals into the cell. The sigma factors are then released from the corresponding anti-sigma factors, and they recruit RNA polymerase to transcribe specific cellulosomal genes. However, it is not clear how the extracellular signals are transduced into the cell by the anti-sigma factors. The anti-sigma factors of C. thermocellum contain an N-terminal intracellular domain, a trans-membrane helix, a periplasmic domain, a proline-rich region which is probably required for crossing the cell wall, and a C-terminal carbohydrate-binding domain or glycoside hydrolase domain. The periplasmic domain may play a key role in signal transduction; however, its three-dimensional structure is still unknown. Here we report the NMR resonance assignments of the periplasmic domain of anti-sigma factor RsgI2 from C. thermocellum as a basis for further structural determination and functional studies.
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Acknowledgments
We thank Professor Sarah Perrett (Institute of Biophysics, Chinese Academy of Sciences) for critically reading the manuscript. This work was supported by the National Basic Research Program of China (973 Program, Grant No. 2011CB707404), the National Natural Science Foundation of China (Grant Nos. 31270784, 31470210, 31171201, and 31070072), and Program for New Century Excellent Talents in University (Grant No. NCET-0900717).
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Ding, X., Chen, C., Cui, Q. et al. Resonance assignments of the periplasmic domain of a cellulose-sensing trans-membrane anti-sigma factor from Clostridium thermocellum . Biomol NMR Assign 9, 321–324 (2015). https://doi.org/10.1007/s12104-015-9601-7
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DOI: https://doi.org/10.1007/s12104-015-9601-7