Proteomics

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Phosphoproteomic analysis of Rhodopseudomonas palustris

ABSTRACT: This study is to compare the phosphoproteome of Rhodopseudomonas palustris under photoheterotrophic and chemoheterotrophic states

INSTRUMENT(S): LTQ Orbitrap, TripleTOF 5600, TripleTOF 6600

ORGANISM(S): Rhodopseudomonas Palustris

SUBMITTER: Chia-Wei Hu  

LAB HEAD: Chia-Wei Hu

PROVIDER: PXD000025 | Pride | 2012-12-12

REPOSITORIES: Pride

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Action DRS
PRIDE_Exp_Complete_Ac_27212.pride.mgf.gz Mgf
PRIDE_Exp_Complete_Ac_27212.pride.mztab.gz Mztab
PRIDE_Exp_Complete_Ac_27212.xml.gz Xml
PRIDE_Exp_Complete_Ac_27213.pride.mgf.gz Mgf
PRIDE_Exp_Complete_Ac_27213.pride.mztab.gz Mztab
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Publications

Phosphoproteomic analysis of Rhodopseudomonas palustris reveals the role of pyruvate phosphate dikinase phosphorylation in lipid production.

Hu Chia-Wei CW   Lin Miao-Hsia MH   Huang Hsuan-Cheng HC   Ku Wei-Chi WC   Yi Tsun-Hsuan TH   Tsai Chia-Feng CF   Chen Yu-Ju YJ   Sugiyama Naoyuki N   Ishihama Yasushi Y   Juan Hsueh-Fen HF   Wu Shih-Hsiung SH  

Journal of proteome research 20121015 11

Rhodopseudomonas palustris (R. palustris) is a purple nonsulfur anoxygenic phototrophic bacterium with metabolic versatility and is able to grow under photoheterotrophic and chemoheterotrophic states. It has uses in carbon management, carbon recycling, hydrogen generation, and lipid production; therefore, it has the potential for bioenergy production and biodegradation. This study is the first to identify the phosphoproteome of R. palustris including 100 phosphopeptides from 54 phosphoproteins  ...[more]

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