An analysis of the proteomic profile for Thermoanaerobacter tengcongensis under optimal culture conditions

The genome of Thermoanaerobacter tengcongensis is estimated to encode 2588 theoretical proteins. In this study, we have vitalized approximately 46% of the theoretical proteome experimentally using a proteomic strategy that combines three different methods, shotgun digestion plus high‐performance liq...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2004-01, Vol.4 (1), p.136-150
Main Authors: Wang, Jingqiang, Xue, Yanfen, Feng, Xiaoli, Li, Xiaolei, Wang, Hao, Li, Wei, Zhao, Caifeng, Cheng, Xiaojie, Ma, Yanhe, Zhou, Peijin, Yin, Jianning, Bhatnagar, Aruni, Wang, Rong, Liu, Siqi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Bacterium
Biological and medical sciences
Chromatography, Liquid
Electrophoresis, Gel, Two-Dimensional
Fundamental and applied biological sciences. Psychology
Gram-Negative Anaerobic Straight, Curved, and Helical Rods - chemistry
Gram-Negative Anaerobic Straight, Curved, and Helical Rods - physiology
Membrane Proteins - chemistry
Miscellaneous
Molecular Sequence Data
Proteins
Proteome - chemistry
Proteome - physiology
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Thermoanaerobacter tengcongensis
Thermophilic
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Summary:The genome of Thermoanaerobacter tengcongensis is estimated to encode 2588 theoretical proteins. In this study, we have vitalized approximately 46% of the theoretical proteome experimentally using a proteomic strategy that combines three different methods, shotgun digestion plus high‐performance liquid chromatography (HPLC) with ion‐trap tandem mass spectrometry (shotgun‐liquid chromatography (LC)/MS), one‐dimensional sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) plus HPLC with ion‐trap tandem mass spectrometry (one‐dimensional electrophoresis (1DE)‐LC/MS), and two‐dimensional gel electrophoresis plus matrix‐assisted laser desorption/ionization‐time of flight‐mass spectrometry (2DE‐MALDI‐TOF‐MS). Of the 1200 proteins identified, as few as 76 proteins were globally found by all three approaches, and notably, most of these proteins were in the soluble fraction. However, there were a number of unique proteins detected by one method only, suggesting that our strategy provides a means toward obtaining a comprehensive view of protein expression profile. Proteins from the major metabolic pathways are strongly represented on the map, and a number of these enzymes were identified by more than one proteomic method. Based upon the proteins identified in the present study, we are able to broaden the understanding of how T. tengcongensis survives under high temperature environment, whereas several of its properties can not be fully explained by genome data.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.200300504