Abstract:
BACKGROUND:Clostridium thermocellum is a Gram-positive thermophilic anaerobic bacterium with the unusual capacity to convert cellulosic biomass into ethanol and hydrogen. Identification and characterization of protein complexes in C. thermocellum are important toward understanding its metabolism and physiology. RESULTS:A two dimensional blue native/SDS-PAGE procedure was developed to separate membrane protein complexes of C. thermocellum. Proteins spots were identified by MALDI-TOF/TOF Mass spectrometry. 24 proteins were identified representing 13 distinct protein complexes, including several putative intact complexes. Interestingly, subunits of both the F1-F0-ATP synthase and the V1-V0-ATP synthase were detected in the membrane sample, indicating C. thermocellum may use alternative mechanisms for ATP generation. CONCLUSION:Two dimensional blue native/SDS-PAGE was used to detect membrane protein complexes in C. thermocellum. More than a dozen putative protein complexes were identified, revealing the simultaneous expression of two sets of ATP synthase. The protocol developed in this work paves the way for further functional characterization of these protein complexes.
journal_name
BMC Microbioljournal_title
BMC microbiologyauthors
Peng Y,Luo Y,Yu T,Xu X,Fan K,Zhao Y,Yang Kdoi
10.1186/1471-2180-11-22subject
Has Abstractpub_date
2011-01-26 00:00:00pages
22issue
1issn
1471-2180pii
1471-2180-11-22journal_volume
11pub_type
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