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A hydrogen-evolving enzyme is present in Frankia sp. R43
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-0536-903X
2004 (English)In: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 236, no 2, 235-240 p.Article in journal (Refereed) Published
Abstract [en]

The ability to evolve hydrogen using methyl viologen as an electron donor was assayed in the nitrogen-fixing actinomycetes Frankia sp. R43 and Frankia sp. KB5. To further examine the nature of hydrogen-evolving enzymes that may be present in these organisms immunological studies were performed. Under anaerobic conditions (both nitrogen-limiting and nitrogen-containing) Frankia sp. R43 but not Frankia sp. KB5 evolved hydrogen,which was not linked to NAD-reducing activity. Immunological analysis of total protein from Frankia sp. R43 and Frankia sp. KB5 using an antiserum raised against Ralstonia eutropha HoxF, recognized an antigen in Frankia sp. R43 but not in Frankia sp. KB5. Immunogold labeling using antibodies raised against the R. eutropha HoxH recognized sites in both hyphae and vesicles of Frankia sp. R43, but not in Frankia sp. KB5. Based on these physiological and immunological findings, we conclude that Frankia sp. R43 has a hydrogen-evolving hydrogenase.

Place, publisher, year, edition, pages
Amsterdam: Elsevier/North-Holland , 2004. Vol. 236, no 2, 235-240 p.
Keyword [en]
Anaerobiosis, Bacterial Proteins/immunology/isolation & purification/metabolism, Blotting; Western, Cupriavidus necator/enzymology/immunology, Frankia/chemistry/*enzymology/immunology, Hydrogen/*metabolism, Hydrogenase/immunology/*metabolism, Hyphae/enzymology, Immunohistochemistry, NAD/metabolism, Paraquat/metabolism
Identifiers
URN: urn:nbn:se:umu:diva-2784DOI: doi:10.1016/j.femsle.2004.05.049PubMedID: 15251202OAI: oai:DiVA.org:umu-2784DiVA: diva2:141053
Available from: 2007-11-16 Created: 2007-11-16 Last updated: 2017-12-14Bibliographically approved
In thesis
1. The Biodiversity of Hydrogenases in Frankia: Characterization, regulation and phylogeny
Open this publication in new window or tab >>The Biodiversity of Hydrogenases in Frankia: Characterization, regulation and phylogeny
2007 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

All the eighteen Frankia strains isolated from ten different actinorhizal host plants showed uptake hydrogenase activity. The activity of this enzyme is further increased by addition of nickel. Nickel also enhanced the degree of hydrogenase transfer into the membranes of Frankia, indicating the role of this metal in the processing of this enzyme. The uptake hydrogenase of Frankia is most probably a Ni-Fe hydrogenase.

Genome characterization revealed the presence of two hydrogenase genes (syntons) in Frankia, which are distinctively separated in all the three available Frankia genomes. Both hydrogenase syntons are also commonly found in other Frankia strains. The structural, regulatory and accessory genes of both hydrogenase synton #1 and #2 are arranged closely together, but in a clearly contrasting organization. Hydrogenase synton #1 and #2 of Frankia are phylogenetically divergent and that hydrogenase synton #1 is probably ancestral among the actinobacteria. Hydrogenase synton #1 (or synton #2) of Frankia sp. CcI3 and F. alni ACN14a are similar in gene arrangement, content and orientation, while the syntons are both reduced and rearranged in Frankia sp. EANpec. The hydrogenases of Frankia sp. CcI3 and F. alni ACN14a are phylogenetically grouped together but never with the Frankia sp. EAN1pec, which is more closely related to the non-Frankia bacteria than Frankia itself. The tree topology is indicative of a probable gene transfer to or from Frankia that occurred before the emergence of Frankia. All of the available evidence points to hydrogenase gene duplication having occurred long before development of the three Frankia lineages. The uptake hydrogenase synton #1 of Frankia is more expressed under free-living conditions whereas hydrogenases synton #2 is mainly involved in symbiotic interactions. The uptake hydrogenase of Frankia can also be manipulated to play a larger role in increasing the efficiency of nitrogen fixation in the root nodules of the host plants, there by minimizing the need for environmentally unfriendly and costly fertilizers.

The hydrogen-evolving hydrogenase activity was recorded in only four Frankia strains: F. alni UGL011101, UGL140102, Frankia sp. CcI3 and R43. After addition of 15mM Nicl2, activity was also detected in F. alni UGL011103, Frankia sp. UGL020602, UGL020603 and 013105. Nickel also increased the activity of hydrogen-evolving hydrogenases in Frankia, indicating that Frankia may have different types of hydrogen-evolving hydrogenases, or that the hydrogen-evolving hydrogenases may at least be regulated differently in different Frankia strains. The fact that Frankia can produce hydrogen is reported only recently. The knowledge of the molecular biology of Frankia hydrogenase is, therefore, of a paramount importance to optimize the system in favor of hydrogen production. Frankia is an attractive candidate in search for an organism efficient in biological hydrogen production since it can produce a considerable amount of hydrogen.

Place, publisher, year, edition, pages
Umeå: Fysiologisk botanik, 2007. 63 p.
Keyword
Biodiversity, Frankia, immunoblotting, gene expression, uptake hydrogenase, hydrogen-evolving hydrogenase, nickel, phylogeny
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-1435 (URN)978-91-7264-444-1 (ISBN)
Public defence
2007-12-07, KB3A9, KBC, Umeå University, Umeå, 10:00 (English)
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Supervisors
Available from: 2007-11-16 Created: 2007-11-16 Last updated: 2011-03-14Bibliographically approved

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Publisher's full textPubMedhttp://dx.doi.org/10.1111/j.1574-6968.2004.tb09652.x

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