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The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis.

Tsu BV, Saier MH - PLoS ONE (2015)

Bottom Line: Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication.Their common origin implies that they share common structural, mechanistic and functional attributes.The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, La Jolla, California, United States of America.

ABSTRACT
The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.

No MeSH data available.


Related in: MedlinePlus

Proposed evolutionary history for the appearance of the eleven recognized families in the LysE superfamily.Protein topologies are indicated with bars representing TMSs and numbers indicating the positions of the TMSs in the proposed TMS primordial protein (in parentheses). Families are indicated by their standard abbreviations while numbers indicate "extra" TMSs outside of their basic 6-TMS unit, resulting from intragenic duplication of the primordial 3TMS precursor. A family abbreviation with a particular topology indicates that at least some members of the family are believed to have this topology.
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pone.0137184.g001: Proposed evolutionary history for the appearance of the eleven recognized families in the LysE superfamily.Protein topologies are indicated with bars representing TMSs and numbers indicating the positions of the TMSs in the proposed TMS primordial protein (in parentheses). Families are indicated by their standard abbreviations while numbers indicate "extra" TMSs outside of their basic 6-TMS unit, resulting from intragenic duplication of the primordial 3TMS precursor. A family abbreviation with a particular topology indicates that at least some members of the family are believed to have this topology.

Mentions: Statistical evidence (Table 2) argued that the TerC, ILT, MntP, CaCA2, NAAT, NicO, GAP and DsbD families are related to the LysE, RhtB and CadD families. Multiple alignments additionally revealed that six TMSs align across all families included in this study. Statistical evidence for homology, multiple alignments of homologues, AveHAS plots, identified internal repeats, MEME/MAST diagrams of conserved motifs, and a proposed evolutionary pathway (evolutionary history) for this expanded superfamily are presented (Figs 1, 2, 3 and 4; S2, S3, S4, S5, S6, S7, S8, S9, S10, S11, S12, S13, S14, S15, S16, S17, S18, S19, S20, S21, S22, S23, S24, S25, S26 and S27 Figs; Tables 1, 2, 3, 4 and 5). In addition, our results confirm topological findings reported in previous studies regarding LysE, RhtB, CadD, MntP, ILT, CaCA2, NAAT and DsbD homologues [1,29,31,32,33,34,35].


The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis.

Tsu BV, Saier MH - PLoS ONE (2015)

Proposed evolutionary history for the appearance of the eleven recognized families in the LysE superfamily.Protein topologies are indicated with bars representing TMSs and numbers indicating the positions of the TMSs in the proposed TMS primordial protein (in parentheses). Families are indicated by their standard abbreviations while numbers indicate "extra" TMSs outside of their basic 6-TMS unit, resulting from intragenic duplication of the primordial 3TMS precursor. A family abbreviation with a particular topology indicates that at least some members of the family are believed to have this topology.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4608589&req=5

pone.0137184.g001: Proposed evolutionary history for the appearance of the eleven recognized families in the LysE superfamily.Protein topologies are indicated with bars representing TMSs and numbers indicating the positions of the TMSs in the proposed TMS primordial protein (in parentheses). Families are indicated by their standard abbreviations while numbers indicate "extra" TMSs outside of their basic 6-TMS unit, resulting from intragenic duplication of the primordial 3TMS precursor. A family abbreviation with a particular topology indicates that at least some members of the family are believed to have this topology.
Mentions: Statistical evidence (Table 2) argued that the TerC, ILT, MntP, CaCA2, NAAT, NicO, GAP and DsbD families are related to the LysE, RhtB and CadD families. Multiple alignments additionally revealed that six TMSs align across all families included in this study. Statistical evidence for homology, multiple alignments of homologues, AveHAS plots, identified internal repeats, MEME/MAST diagrams of conserved motifs, and a proposed evolutionary pathway (evolutionary history) for this expanded superfamily are presented (Figs 1, 2, 3 and 4; S2, S3, S4, S5, S6, S7, S8, S9, S10, S11, S12, S13, S14, S15, S16, S17, S18, S19, S20, S21, S22, S23, S24, S25, S26 and S27 Figs; Tables 1, 2, 3, 4 and 5). In addition, our results confirm topological findings reported in previous studies regarding LysE, RhtB, CadD, MntP, ILT, CaCA2, NAAT and DsbD homologues [1,29,31,32,33,34,35].

Bottom Line: Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication.Their common origin implies that they share common structural, mechanistic and functional attributes.The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, La Jolla, California, United States of America.

ABSTRACT
The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.

No MeSH data available.


Related in: MedlinePlus