L
Louis S. Tisa
Researcher at University of New Hampshire
Publications - 171
Citations - 4723
Louis S. Tisa is an academic researcher from University of New Hampshire. The author has contributed to research in topics: Frankia & Actinorhizal plant. The author has an hindex of 37, co-authored 165 publications receiving 4145 citations. Previous affiliations of Louis S. Tisa include University of North Bengal & Savannah River National Laboratory.
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Journal ArticleDOI
Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography.
Philippe Normand,Pascal Lapierre,Louis S. Tisa,Johann Peter Gogarten,Nicole Alloisio,Emilie Bagnarol,Carla A. Bassi,Alison M. Berry,Derek M. Bickhart,Nathalie Choisne,Arnaud Couloux,Benoit Cournoyer,Stéphane Cruveiller,Vincent Daubin,Nadia Demange,Maria Pilar Francino,Eugene Goltsman,Ying Huang,Olga R. Kopp,Laurent Labarre,Alla Lapidus,Céline Lavire,J Maréchal,Michele Martinez,Juliana E. Mastronunzio,Beth C. Mullin,James Niemann,Pierre Pujic,Tania Rawnsley,Zoé Rouy,Chantal Schenowitz,Anita Sellstedt,Fernando Tavares,Jeffrey P. Tomkins,David Vallenet,Claudio Valverde,Luis Gabriel Wall,Ying Wang,Claudine Médigue,David R. Benson +39 more
TL;DR: The results support the idea that major genome expansions as well as reductions can occur in facultative symbiotic soil bacteria as they respond to new environments in the context of their symbioses.
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Melanin production and use as a soluble electron shuttle for Fe(III) oxide reduction and as a terminal electron acceptor by Shewanella algae BrY.
TL;DR: Melanin produced by S. algae BrY imparts increased versatility to this organism as a soluble Fe(III) reductant, an electron conduit for iron mineral reduction, and a sole terminal electron acceptor that supports growth.
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Molecular characterization of an anion pump. The ArsB protein is the membrane anchor for the ArsA protein.
Louis S. Tisa,Barry P. Rosen +1 more
TL;DR: Evidence is presented showing that expression of the arsB gene is required to anchor the ArsA protein to the inner membrane, and binding studies with purified ArsA to membranes with and without the arSB gene product confirm this requirement.
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Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase.
TL;DR: To localize individual segments of the ArsB protein, a ternary fusion method was developed, where portions of the arsB gene were inserted in-frame between the coding regions for two heterologous proteins, in this case a portion of a newly identified arsD gene and the blaM sequence encoding the mature beta-lactamase.
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Identification of the metalloregulatory element of the plasmid-encoded arsenical resistance operon
TL;DR: The regulatory region of the plasmid-encoded arsenical resistance (ars) operon was cloned as a 727-bp EcoRI-HindIII fragment, indicating that the fragment carried a regulatory gene, the arsR gene, which was used to produce antibodies specific for the ArsR protein.