Premium
Proteome Analysis of Enriched Heterocysts from Two Hydrogenase Mutants from Anabaena sp. PCC 7120
Author(s) -
Kourpa Katerina,
Manarolaki Eftychia,
Lyratzakis Alexandros,
Strataki Vasso,
Rupprecht Fiona,
Langer Julian D.,
Tsiotis Georgios
Publication year - 2019
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201800332
Subject(s) - heterocyst , hydrogenase , cyanobacteria , proteome , anabaena , biochemistry , nitrogenase , mutant , biology , proteomics , nitrogen fixation , enzyme , chemistry , bacteria , gene , genetics
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 (Δ hupL ) and the bidirectional hydrogenase (Δ hoxH ) in previous studies. Here the proteomic differences of enriched heterocysts between these mutants cultured in N 2 ‐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 Δ hupL and 117 proteins in the Δ hoxH 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.