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Posttranslational modification of a vanadium nitrogenase.

Heiniger EK, Harwood CS - Microbiologyopen (2015)

Bottom Line: However, the posttranslational modification of vanadium nitrogenase has not been reported.Vanadium nitrogenase is not found in all strains of R. palustris, suggesting that it may have been acquired by horizontal gene transfer.Also, phylogenetic analyses of the three nitrogenases suggest that VnfH, the target of ADP-ribosylation, may be the product of a gene duplication of nifH, the molybdenum nitrogenase homolog.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, University of Washington, Seattle, Washington, 98195.

No MeSH data available.


Related in: MedlinePlus

Evolutionary relationships of all three nitrogenase isozymes show disparate origins of the VnfH proteins compared to VnfD (Fig.3). The evolutionary histories of NifH, VnfH, and AnfH were inferred as described for Fig.3. The analysis involved 24 amino acid sequences. All positions containing gaps and missing data were eliminated. There were a total of 224 positions in the final dataset. VnfH in R. palustris is more related to the NifH protein of R. palustris than to any other NifH homolog.
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fig04: Evolutionary relationships of all three nitrogenase isozymes show disparate origins of the VnfH proteins compared to VnfD (Fig.3). The evolutionary histories of NifH, VnfH, and AnfH were inferred as described for Fig.3. The analysis involved 24 amino acid sequences. All positions containing gaps and missing data were eliminated. There were a total of 224 positions in the final dataset. VnfH in R. palustris is more related to the NifH protein of R. palustris than to any other NifH homolog.

Mentions: Fe-nitrogenase enzymes have been shown to be posttranslationally modified in other species of purple nonsulfur bacteria (Lowery et al. 1986; Masepohl et al. 1993). The vanadium isozyme has not been described in other species of purple nonsulfur bacteria and is present in only some strains of R. palustris. It is found primarily in Azotobacter species, cyanobacteria, and methanogens – phyla that do not have a DraT posttranslational mechanism of nitrogenase control. To probe the evolutionary history of the R. palustris alternative nitrogenases, we built phylogenetic trees using neighbor-joining. The tree of the D catalytic subunits of nitrogenases suggests that the three R. palustris nitrogenase isozymes (NifD, VnfD, and AnfD) are most closely related to the three corresponding nitrogenase isozymes from A. vinelandii DJ (Fig3). A tree of nitrogenase reductase (H) subunits gives a slightly different picture, however, and shows that VnfH from R. palustris is most closely related to the R. palustris NifH protein, suggesting that VnfH is the product of a gene duplication event (Fig.4).


Posttranslational modification of a vanadium nitrogenase.

Heiniger EK, Harwood CS - Microbiologyopen (2015)

Evolutionary relationships of all three nitrogenase isozymes show disparate origins of the VnfH proteins compared to VnfD (Fig.3). The evolutionary histories of NifH, VnfH, and AnfH were inferred as described for Fig.3. The analysis involved 24 amino acid sequences. All positions containing gaps and missing data were eliminated. There were a total of 224 positions in the final dataset. VnfH in R. palustris is more related to the NifH protein of R. palustris than to any other NifH homolog.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4554455&req=5

fig04: Evolutionary relationships of all three nitrogenase isozymes show disparate origins of the VnfH proteins compared to VnfD (Fig.3). The evolutionary histories of NifH, VnfH, and AnfH were inferred as described for Fig.3. The analysis involved 24 amino acid sequences. All positions containing gaps and missing data were eliminated. There were a total of 224 positions in the final dataset. VnfH in R. palustris is more related to the NifH protein of R. palustris than to any other NifH homolog.
Mentions: Fe-nitrogenase enzymes have been shown to be posttranslationally modified in other species of purple nonsulfur bacteria (Lowery et al. 1986; Masepohl et al. 1993). The vanadium isozyme has not been described in other species of purple nonsulfur bacteria and is present in only some strains of R. palustris. It is found primarily in Azotobacter species, cyanobacteria, and methanogens – phyla that do not have a DraT posttranslational mechanism of nitrogenase control. To probe the evolutionary history of the R. palustris alternative nitrogenases, we built phylogenetic trees using neighbor-joining. The tree of the D catalytic subunits of nitrogenases suggests that the three R. palustris nitrogenase isozymes (NifD, VnfD, and AnfD) are most closely related to the three corresponding nitrogenase isozymes from A. vinelandii DJ (Fig3). A tree of nitrogenase reductase (H) subunits gives a slightly different picture, however, and shows that VnfH from R. palustris is most closely related to the R. palustris NifH protein, suggesting that VnfH is the product of a gene duplication event (Fig.4).

Bottom Line: However, the posttranslational modification of vanadium nitrogenase has not been reported.Vanadium nitrogenase is not found in all strains of R. palustris, suggesting that it may have been acquired by horizontal gene transfer.Also, phylogenetic analyses of the three nitrogenases suggest that VnfH, the target of ADP-ribosylation, may be the product of a gene duplication of nifH, the molybdenum nitrogenase homolog.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, University of Washington, Seattle, Washington, 98195.

No MeSH data available.


Related in: MedlinePlus