Revealing the Functions of the Transketolase Enzyme Isoforms in Rhodopseudomonas palustris Using a Systems Biology Approach 英文参考文献.docVIP

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Revealing the Functions of the Transketolase Enzyme Isoforms in Rhodopseudomonas palustris Using a Systems Biology Approach 英文参考文献.doc

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Revealing the Functions of the Transketolase Enzyme Isoforms in Rhodopseudomonas palustris Using a Systems Biology Approach 英文参考文献

RevealingtheFunctionsoftheTransketolaseEnzyme IsoformsinRhodopseudomonaspalustrisUsinga SystemsBiologyApproach Chia-WeiHu1,Ya-LingChang1,ShiangJiuunChen2,Ling-LongKuo-Huang2,3,JamesC.Liao4 ,Hsuan- ChengHuang5*,Hsueh-FenJuan1,2* 1Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, Taiwan, 2Department of Life Science, National Taiwan University, Taipei, Taiwan, 3Institute of Ecology and Evolutionary Biology, National Taiwan University, Taipei, Taiwan, 4Department of Chemical and Biomolecular Engineering, University of California,LosAngeles,CA,UnitedStatesofAmerica,5InstituteofBiomedicalInformaticsandCenterforSystemsandSyntheticBiology,NationalYang-MingUniversity, Taipei,Taiwan Abstract Background: Rhodopseudomonas palustris (R. palustris) is a purple non-sulfur anoxygenic phototrophic bacterium that belongstotheclassofproteobacteria.Itiscapableofabsorbingatmosphericcarbondioxideandconvertingittobiomass viatheprocessofphotosynthesisandtheCalvin–Benson–Bassham(CBB)cycle.Transketolaseisakeyenzymeinvolvedin the CBB cycle. Here, we reveal the functions of transketolase isoforms I and II in R. palustris using a systems biology approach. Methodology/PrincipalFindings:Bymeasuringgrowthability,wefoundthattransketolasecouldenhancetheautotrophic growth and biomass production of R. palustris. Microarray and real-time quantitative PCR revealed that transketolase isoforms IandII wereinvolvedindifferent carbonmetabolicpathways. Inaddition,immunogoldstainingdemonstrated that the two transketolase isoforms had different spatial localizations: transketolase I was primarily associated with the intracytoplasmic membrane (ICM) but transketolase II was mostly distributed in the cytoplasm. Comparative proteomic analysisandnetworkconstructionoftransketolaseover-expressionandnegativecontrol(NC)strainsrevealedthatprotein folding,transcriptionalregulation,aminoacidtransportandCBBcycle-associatedcarbonmetabolismwereenrichedinthe transketolase I over-expressed str