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MamA as a Model Protein for Structure-Based Insight into the Evolutionary Origins of Magnetotactic Bacteria.

Zeytuni N, Cronin S, Lefèvre CT, Arnoux P, Baran D, Shtein Z, Davidov G, Zarivach R - PLoS ONE (2015)

Bottom Line: As such, this allows us to perform structural- and phylogenetic-based analyses using a variety of previously determined MamA from a diverse range of MTB species across various phylogenetic groups.We found that MamA has remained remarkably constant throughout evolution with minimal change between different taxa despite sequence variations.These findings, coupled with the generation of phylogenetic trees using both amino acid sequences and 16S rRNA, indicate that magnetotaxis likely did not spread via horizontal gene transfer and instead has a significantly earlier, primordial origin.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences and The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer Sheva, Israel.

ABSTRACT
MamA is a highly conserved protein found in magnetotactic bacteria (MTB), a diverse group of prokaryotes capable of navigating according to magnetic fields - an ability known as magnetotaxis. Questions surround the acquisition of this magnetic navigation ability; namely, whether it arose through horizontal or vertical gene transfer. Though its exact function is unknown, MamA surrounds the magnetosome, the magnetic organelle embedding a biomineralised nanoparticle and responsible for magnetotaxis. Several structures for MamA from a variety of species have been determined and show a high degree of structural similarity. By determining the structure of MamA from Desulfovibrio magneticus RS-1 using X-ray crystallography, we have opened up the structure-sequence landscape. As such, this allows us to perform structural- and phylogenetic-based analyses using a variety of previously determined MamA from a diverse range of MTB species across various phylogenetic groups. We found that MamA has remained remarkably constant throughout evolution with minimal change between different taxa despite sequence variations. These findings, coupled with the generation of phylogenetic trees using both amino acid sequences and 16S rRNA, indicate that magnetotaxis likely did not spread via horizontal gene transfer and instead has a significantly earlier, primordial origin.

No MeSH data available.


ConSurf analysis shows a high degree of structural conservation between ArsTM and MamA from alternative species, though this is largely limited to the concave surface and a cluster around the fifth TPR and the C-terminal.All sequences used in this analysis are shown in the multiple sequence alignment of S2 Fig.
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pone.0130394.g002: ConSurf analysis shows a high degree of structural conservation between ArsTM and MamA from alternative species, though this is largely limited to the concave surface and a cluster around the fifth TPR and the C-terminal.All sequences used in this analysis are shown in the multiple sequence alignment of S2 Fig.

Mentions: These findings are reinforced by analysis using ConSurf [25,26], a tool for determining evolutionary conservation of amino acids using phylogenetics, which displayed a high degree of structural conservation between ArsTM and MamA from other species of MTB (Fig 2). In particular, the fifth TPR around the C-terminus is highly conserved, as well as the concave surface of the protein. Conversely, the backbone of the monomer is distinctly unconserved displaying only a few small conserved patches that are clusters of single or double residues.


MamA as a Model Protein for Structure-Based Insight into the Evolutionary Origins of Magnetotactic Bacteria.

Zeytuni N, Cronin S, Lefèvre CT, Arnoux P, Baran D, Shtein Z, Davidov G, Zarivach R - PLoS ONE (2015)

ConSurf analysis shows a high degree of structural conservation between ArsTM and MamA from alternative species, though this is largely limited to the concave surface and a cluster around the fifth TPR and the C-terminal.All sequences used in this analysis are shown in the multiple sequence alignment of S2 Fig.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4482739&req=5

pone.0130394.g002: ConSurf analysis shows a high degree of structural conservation between ArsTM and MamA from alternative species, though this is largely limited to the concave surface and a cluster around the fifth TPR and the C-terminal.All sequences used in this analysis are shown in the multiple sequence alignment of S2 Fig.
Mentions: These findings are reinforced by analysis using ConSurf [25,26], a tool for determining evolutionary conservation of amino acids using phylogenetics, which displayed a high degree of structural conservation between ArsTM and MamA from other species of MTB (Fig 2). In particular, the fifth TPR around the C-terminus is highly conserved, as well as the concave surface of the protein. Conversely, the backbone of the monomer is distinctly unconserved displaying only a few small conserved patches that are clusters of single or double residues.

Bottom Line: As such, this allows us to perform structural- and phylogenetic-based analyses using a variety of previously determined MamA from a diverse range of MTB species across various phylogenetic groups.We found that MamA has remained remarkably constant throughout evolution with minimal change between different taxa despite sequence variations.These findings, coupled with the generation of phylogenetic trees using both amino acid sequences and 16S rRNA, indicate that magnetotaxis likely did not spread via horizontal gene transfer and instead has a significantly earlier, primordial origin.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences and The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer Sheva, Israel.

ABSTRACT
MamA is a highly conserved protein found in magnetotactic bacteria (MTB), a diverse group of prokaryotes capable of navigating according to magnetic fields - an ability known as magnetotaxis. Questions surround the acquisition of this magnetic navigation ability; namely, whether it arose through horizontal or vertical gene transfer. Though its exact function is unknown, MamA surrounds the magnetosome, the magnetic organelle embedding a biomineralised nanoparticle and responsible for magnetotaxis. Several structures for MamA from a variety of species have been determined and show a high degree of structural similarity. By determining the structure of MamA from Desulfovibrio magneticus RS-1 using X-ray crystallography, we have opened up the structure-sequence landscape. As such, this allows us to perform structural- and phylogenetic-based analyses using a variety of previously determined MamA from a diverse range of MTB species across various phylogenetic groups. We found that MamA has remained remarkably constant throughout evolution with minimal change between different taxa despite sequence variations. These findings, coupled with the generation of phylogenetic trees using both amino acid sequences and 16S rRNA, indicate that magnetotaxis likely did not spread via horizontal gene transfer and instead has a significantly earlier, primordial origin.

No MeSH data available.