Immunolocalization of the uptake hydrogenase in the marine cyanobacterium Lyngbya majuscula CCAP 1446/4 and two Nostoc strains

In N₂-fixing cyanobacteria, the reduction of N₂ to NH₃ is coupled with the production of molecular hydrogen, which is rapidly consumed by an uptake hydrogenase, an enzyme that is present in almost all diazotrophic cyanobacteria. The cellular and subcellular localization of the cyanobacterial uptake...

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Bibliographic Details
Published in:FEMS microbiology letters 2009-03, Vol.292 (1), p.57-62
Main Authors: Seabra, Rui, Santos, Arlete, Pereira, Sara, Moradas-Ferreira, Pedro, Tamagnini, Paula
Format: Article
Language:English
Subjects:
Bacterial Proteins - analysis
Bacteriology
Biological and medical sciences
Cyanobacteria
Cyanobacteria - chemistry
Cyanobacteria - enzymology
Cyanophyta
Fundamental and applied biological sciences. Psychology
immunolocalization
Lyngbya majuscula
Metabolism. Enzymes
Microbiology
Microscopy, Immunoelectron
Nostoc
Nostoc - chemistry
Nostoc - enzymology
Nostoc punctiforme
Oxidoreductases - analysis
Permeability, membrane transport, intracellular transport
TEM
Thylakoids - chemistry
uptake hydrogenase
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Summary:In N₂-fixing cyanobacteria, the reduction of N₂ to NH₃ is coupled with the production of molecular hydrogen, which is rapidly consumed by an uptake hydrogenase, an enzyme that is present in almost all diazotrophic cyanobacteria. The cellular and subcellular localization of the cyanobacterial uptake hydrogenase remains uncertain, and it is definitely strain dependent. Previous studies focused mainly on heterocystous cyanobacteria and used heterologous antisera. The present work represents the first effort to establish the subcellular localization of the uptake hydrogenase in a N₂-fixing filamentous nonheterocystous cyanobacterium, Lyngbya majuscula CCAP 1446/4, using the first antiserum produced against a cyanobacterial uptake hydrogenase. The data obtained revealed higher specific labelling associated with the thylakoid membranes of L. majuscula, reinforcing the idea that the cyanobacterial uptake hydrogenase is indeed a membrane-bound protein. For comparative purposes, the localization of the uptake hydrogenase was also investigated in two distinct heterocystous cyanobacterial strains, and while in Nostoc sp. PCC 7120 the labelling was only observed in the heterocysts, in Nostoc punctiforme, the presence of uptake hydrogenase antigens was detected in both the vegetative cells and heterocysts, corresponding most probably to an inactive and an active form of the enzyme.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2008.01471.x