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Proteome Analysis of Enriched Heterocysts from Two Hydrogenase Mutants from Anabaena sp. PCC 7120

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Rupprecht,  Fiona A.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Langer,  Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Citation

Kourpa, K., Manarolaki, E., Lyratzakis, A., Strataki, V., Rupprecht, F. A., Langer, J. D., et al. (2019). Proteome Analysis of Enriched Heterocysts from Two Hydrogenase Mutants from Anabaena sp. PCC 7120. Proteomics, 19: 1800332. doi:10.1002/pmic.201800332.


Cite as: http://hdl.handle.net/21.11116/0000-0004-A0A7-A
Abstract
Cyanobacteria are oxygenic photosynthetic prokaryotes and play a crucial role in the Earth's carbon and nitrogen cycles. The photoautotrophic cyanobacterium Anabaena sp. PCC 7120 has the ability to fix atmospheric nitrogen in heterocysts and produce hydrogen as a byproduct through a nitrogenase. In order to improve hydrogen production, mutants from Anabaena sp. PCC 7120 are constructed by inactivation of the uptake hydrogenase (ΔhupL) and the bidirectional hydrogenase (ΔhoxH) in previous studies. Here the proteomic differences of enriched heterocysts between these mutants cultured in N2-fixing conditions are investigated. Using a label-free quantitative proteomics approach, a total of 2728 proteins are identified and it is found that 79 proteins are differentially expressed in the ΔhupL and 117 proteins in the ΔhoxH variant. The results provide for the first time comprehensive information on proteome regulation of the uptake hydrogenase and the bidirectional hydrogenase, as well as systematic data on the hydrogen related metabolism in Anabaena sp. PCC 7120.