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Dive into the research topics where Timothy D. Hey is active.

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Featured researches published by Timothy D. Hey.


Science | 2010

Photorhabdus luminescens Toxins ADP-Ribosylate Actin and RhoA to Force Actin Clustering

Alexander E. Lang; Gudula Schmidt; Andreas Schlosser; Timothy D. Hey; Ignacio M. Larrinua; Joel J. Sheets; Hans Georg Mannherz; Klaus Aktories

Tripartite Toxin Luminescent bacterial symbionts of nematode worms that attack insects have long stirred interest in their possibilities for biological control. The bacteria produce a family of toxins composed of at least three subunits that resemble a widely occurring class of bacterial toxins also produced by human pathogens. Lang et al. (p. 1139) have elucidated the mode of action and structural interactions of some of these tripartite protein toxins and found that they poison the cells actin cytoskeleton by catalyzing unusual reactions. One toxin mediated adenosine diphosphate (ADP)–ribosylation at threonine-148 to cause actin polymerization, another ADP-ribosylated Rho protein at glutamine-63, and both synergized to cause actin clustering and cell paralysis. A bacterial toxin targets and modifies the actin cytoskeleton in insect larvae. The bacterium Photorhabdus luminescens is mutualistically associated with entomopathogenetic nematodes. These nematodes invade insect larvae and release the bacteria from their intestine, which kills the insects through the action of toxin complexes. We elucidated the mode of action of two of these insecticidal toxins from P. luminescens. We identified the biologically active components TccC3 and TccC5 as adenosine diphosphate (ADP)–ribosyltransferases, which modify unusual amino acids. TccC3 ADP-ribosylated threonine-148 of actin, resulting in actin polymerization. TccC5 ADP-ribosylated Rho guanosine triphosphatase proteins at glutamine-61 and glutamine-63, inducing their activation. The concerted action of both toxins inhibited phagocytosis of target insect cells and induced extensive intracellular polymerization and clustering of actin. Several human pathogenic bacteria produce related toxins.


PLOS ONE | 2013

Bacillus thuringiensis Cry34Ab1/Cry35Ab1 Interactions with Western Corn Rootworm Midgut Membrane Binding Sites

Huarong Li; Monica Britt Olson; Gaofeng Lin; Timothy D. Hey; Sek Yee Tan; Kenneth E. Narva

Background Bacillus thuringiensis (Bt) Cry34Ab1/Cry35Ab1 are binary insecticidal proteins that are co-expressed in transgenic corn hybrids for control of western corn rootworm, Diabrotica virgifera virgifera LeConte. Bt crystal (Cry) proteins with limited potential for field-relevant cross-resistance are used in combination, along with non-transgenic corn refuges, as a strategy to delay development of resistant rootworm populations. Differences in insect midgut membrane binding site interactions are one line of evidence that Bt protein mechanisms of action differ and that the probability of receptor-mediated cross-resistance is low. Methodology/Principal Findings Binding site interactions were investigated between Cry34Ab1/Cry35Ab1 and coleopteran active insecticidal proteins Cry3Aa, Cry6Aa, and Cry8Ba on western corn rootworm midgut brush border membrane vesicles (BBMV). Competitive binding of radio-labeled proteins to western corn rootworm BBMV was used as a measure of shared binding sites. Our work shows that 125I-Cry35Ab1 binds to rootworm BBMV, Cry34Ab1 enhances 125I-Cry35Ab1 specific binding, and that 125I-Cry35Ab1 with or without unlabeled Cry34Ab1 does not share binding sites with Cry3Aa, Cry6Aa, or Cry8Ba. Two primary lines of evidence presented here support the lack of shared binding sites between Cry34Ab1/Cry35Ab1 and the aforementioned proteins: 1) No competitive binding to rootworm BBMV was observed for competitor proteins when used in excess with 125I-Cry35Ab1 alone or combined with unlabeled Cry34Ab1, and 2) No competitive binding to rootworm BBMV was observed for unlabeled Cry34Ab1 and Cry35Ab1, or a combination of the two, when used in excess with 125I-Cry3Aa, or 125I-Cry8Ba. Conclusions/Significance Combining two or more insecticidal proteins active against the same target pest is one tactic to delay the onset of resistance to either protein. We conclude that Cry34Ab1/Cry35Ab1 are compatible with Cry3Aa, Cry6Aa, or Cry8Ba for deployment as insect resistance management pyramids for in-plant control of western corn rootworm.


Archive | 1995

Ribosome-inactivating proteins, inactive precursor forms thereof, a process for making and a method of using

Terence A. Walsh; Timothy D. Hey; Alice E. R. Morgan


Archive | 2004

Mixing and matching TC proteins for pest control

Timothy D. Hey; Amanda D. Schleper; Scott Bevan; Scott B. Bintrim; Jon C. Mitchell; Ze Sheng Li; Weiting Ni; Baolong Zhu; Donald J. Merlo; Patricia C. Apel-Birkhold; Thomas Meade


Archive | 1999

Regulatory sequences useful for gene expression in plant embryo tissue

Katherine Armstrong; Dayakar Pareddy; Aaron T. Woosley; Beth Rubin-Wilson; Timothy D. Hey; Otto Folkerts; Kelley A. Smith


Archive | 1998

Nucleotide sequences of genes encoding sink protein and uses thereof for improving the nutritional quality of feeds

Timothy D. Hey; Ann Owens Merlo; Terence A. Walsh


Archive | 2009

Constructs for expressing herbicide tolerance genes, related plants, and related trait combinations

Justin M. Lira; Terry R. Wright; Timothy D. Hey; Tonya Strange Moynahan; Lisa W. Baker


BMC Biology | 2016

The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins

Alexey Dementiev; Jason Board; Anand Sitaram; Timothy D. Hey; Matthew S. Kelker; Xiaoping Xu; Yan Hu; Cristian Vidal-Quist; Vimbai Chikwana; Samantha Griffin; David McCaskill; Nick X. Wang; Shao-Ching Hung; Michael K. Chan; Marianne M. Lee; Jessica Hughes; Alice Wegener; Raffi V. Aroian; Kenneth E. Narva; Colin Berry


Archive | 2005

Insecticidal toxin complex fusion proteins

Timothy D. Hey; Thomas Meade; Stephanie L. Burton; Donald J. Merlo; Qihua Cai; Haley Jo Moon; Joel J. Sheets; Aaron T. Woosley


Archive | 2009

Nematode-resistant plants, and modified bacillus thuringiensis cry genes and proteins

Timothy D. Hey; Aaron T. Woosley; Kenneth E. Narva

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