J
John F. Beckmann
Researcher at Auburn University
Publications - 25
Citations - 1207
John F. Beckmann is an academic researcher from Auburn University. The author has contributed to research in topics: Wolbachia & Cytoplasmic incompatibility. The author has an hindex of 10, co-authored 17 publications receiving 855 citations. Previous affiliations of John F. Beckmann include University of Minnesota & Yale University.
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Journal ArticleDOI
Prophage WO genes recapitulate and enhance Wolbachia -induced cytoplasmic incompatibility
Daniel P. LePage,Jason A. Metcalf,Sarah R. Bordenstein,Jungmin On,Jessamyn I. Perlmutter,J. Dylan Shropshire,Emily M. Layton,Lisa J. Funkhouser-Jones,John F. Beckmann,Seth R. Bordenstein +9 more
TL;DR: Comparison and transgenic approaches are used to demonstrate that two differentially transcribed, co-diverging genes in the eukaryotic association module of prophage WO from Wolbachia strain wMel recapitulate and enhance cytoplasmic incompatibility.
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A Wolbachia Deubiquitylating Enzyme Induces Cytoplasmic Incompatibility
TL;DR: It is shown that a Wolbachia deubiquitylating enzyme (DUB) induces cytoplasmic incompatibility (CI), a gene-drive mechanism impacting population structure and causing reproductive isolation, and new methods for insect control are suggested.
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Detection of the Wolbachia protein WPIP0282 in mosquito spermathecae: implications for cytoplasmic incompatibility.
John F. Beckmann,Ann M. Fallon +1 more
TL;DR: The absence of wP Pip_0282 and wPip_0283 homologs from genomes of Wolbachia in filarial nematodes, as well as other members of the Rickettsiales, suggests a role as a candidate CI effector.
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The Toxin–Antidote Model of Cytoplasmic Incompatibility: Genetics and Evolutionary Implications
John F. Beckmann,Manon Bonneau,Hongli Chen,Mark Hochstrasser,Denis Poinsot,Hervé Merçot,Mylène Weill,Mathieu Sicard,Sylvain Charlat +8 more
TL;DR: The tight association of the CI genes with prophages provides clues to the possible evolutionary origin of this phenomenon and the levels of selection at play.
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Substrate specificity of the ubiquitin and Ubl proteases.
TL;DR: Recent structural and biochemical studies that provide insights into mechanisms of substrate specificity among various DUBs and ULPs are summarized and the unexpected specificities of non-eukaryotic proteases in these families are discussed.