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  • 1
    Publication Date: 2014-12-04
    Description: Horizontal gene transfer allows organisms to rapidly acquire adaptive traits. Although documented instances of horizontal gene transfer from bacteria to eukaryotes remain rare, bacteria represent a rich source of new functions potentially available for co-option. One benefit that genes of bacterial origin could provide to eukaryotes is the capacity to produce antibacterials, which have evolved in prokaryotes as the result of eons of interbacterial competition. The type VI secretion amidase effector (Tae) proteins are potent bacteriocidal enzymes that degrade the cell wall when delivered into competing bacterial cells by the type VI secretion system. Here we show that tae genes have been transferred to eukaryotes on at least six occasions, and that the resulting domesticated amidase effector (dae) genes have been preserved for hundreds of millions of years through purifying selection. We show that the dae genes acquired eukaryotic secretion signals, are expressed within recipient organisms, and encode active antibacterial toxins that possess substrate specificity matching extant Tae proteins of the same lineage. Finally, we show that a dae gene in the deer tick Ixodes scapularis limits proliferation of Borrelia burgdorferi, the aetiologic agent of Lyme disease. Our work demonstrates that a family of horizontally acquired toxins honed to mediate interbacterial antagonism confers previously undescribed antibacterial capacity to eukaryotes. We speculate that the selective pressure imposed by competition between bacteria has produced a reservoir of genes encoding diverse antimicrobial functions that are tailored for co-option by eukaryotic innate immune systems.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4713192/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4713192/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chou, Seemay -- Daugherty, Matthew D -- Peterson, S Brook -- Biboy, Jacob -- Yang, Youyun -- Jutras, Brandon L -- Fritz-Laylin, Lillian K -- Ferrin, Michael A -- Harding, Brittany N -- Jacobs-Wagner, Christine -- Yang, X Frank -- Vollmer, Waldemar -- Malik, Harmit S -- Mougous, Joseph D -- AI080609/AI/NIAID NIH HHS/ -- AI083640/AI/NIAID NIH HHS/ -- BB/I020012/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- R01 AI080609/AI/NIAID NIH HHS/ -- R01 AI083640/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2015 Feb 5;518(7537):98-101. doi: 10.1038/nature13965. Epub 2014 Nov 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington School of Medicine, Seattle, Washington 98195, USA. ; 1] Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA [2] Howard Hughes Medical Institute, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA. ; Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4AX, UK. ; Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA. ; 1] Microbial Sciences Institute, Yale University, New Haven, Connecticut 06516, USA [2] Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06516, USA. ; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA. ; 1] Microbial Sciences Institute, Yale University, New Haven, Connecticut 06516, USA [2] Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06516, USA [3] Department of Microbial Pathogenesis, Yale University, New Haven, Connecticut 06516, USA [4] Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06516, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25470067" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/genetics/metabolism/secretion ; Animals ; Bacteria/cytology/*enzymology/*genetics/immunology ; Bacterial Secretion Systems ; Bacterial Toxins/*genetics/metabolism ; Borrelia burgdorferi/cytology/growth & development/immunology ; Cell Wall/metabolism ; Conserved Sequence/genetics ; Eukaryota/*genetics/*immunology/metabolism ; Gene Transfer, Horizontal/*genetics ; Genes, Bacterial/*genetics ; *Immunity, Innate/genetics ; Ixodes/genetics/immunology/metabolism/microbiology ; Phylogeny ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Keywords: IN-VITRO ; CELL ; SYSTEM ; ESCHERICHIA-COLI ; cytoskeleton ; vimentin ; FIBRILLARY ACIDIC PROTEIN ; HEAD DOMAIN ; BINDING-PROTEIN ; COILED-COIL ; TAIL DOMAIN ; CELL ARCHITECTURE ; bacterial cytoskeleton ; Caulobacter crescentus ; CAULOBACTER-CRESCENTUS ; cell curvature ; crescentin
    Abstract: Crescentin is a bacterial filament-forming protein that exhibits domain organization features found in metazoan intermediate filament (IF) proteins. Structure-function studies of eukaryotic IFs have been hindered by a lack of simple genetic systems and easily quantifiable phenotypes. Here we exploit the characteristic localization of the crescentin structure along the inner curvature of Caulobacter crescentus cells and the loss of cell curvature associated with impaired crescentin function to analyze the importance of the domain organization of crescentin. By combining biochemistry and ultrastructural analysis in vitro with cellular localization and functional studies, we show that crescentin requires its distinctive domain organization, and furthermore that different structural elements have distinct structural and functional contributions. The head domain can be functionally subdivided into two subdomains; the first (amino-terminal) is required for function but not assembly, while the second is necessary for structure assembly. The rod domain is similarly required for structure assembly, and the linker L1 appears important to prevent runaway assembly into nonfunctional aggregates. The data also suggest that the stutter and the tail domain have critical functional roles in stabilizing crescentin structures against disassembly by monovalent cations in the cytoplasm. This study suggests that the IF-like behavior of crescentin is a consequence of its domain organization, implying that the IF protein layout is an adaptable cytoskeletal motif, much like the actin and tubulin folds, that is broadly exploited for various functions throughout life from bacteria to humans. (C) 2011 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 21360832
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  • 3
    Publication Date: 2018-11-09
    Description: We describe a general computational approach to designing self-assembling helical filaments from monomeric proteins and use this approach to design proteins that assemble into micrometer-scale filaments with a wide range of geometries in vivo and in vitro. Cryo–electron microscopy structures of six designs are close to the computational design models. The filament building blocks are idealized repeat proteins, and thus the diameter of the filaments can be systematically tuned by varying the number of repeat units. The assembly and disassembly of the filaments can be controlled by engineered anchor and capping units built from monomers lacking one of the interaction surfaces. The ability to generate dynamic, highly ordered structures that span micrometers from protein monomers opens up possibilities for the fabrication of new multiscale metamaterials.
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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