U.S. Department of Health and Human Services

Laboratory of Molecular Biology

Susan K. Buchanan, Ph.D., Chief

​Research Images

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TitleDescriptionImage
Introduction to the Hermes transposon #1This image depicts some of the reasons why we study Hermes transposition.Enlarge
Introduction to the Hermes transposon #2This image depicts a schematic representation of the cut-and-paste reaction catalyzed by the Hermes transposase. For simplicity, the reactions are shown for only one end (the so-called Left End) of the transposon, so you must imagine the identical reactions are carried out on the Right End (not shown). For comparison, the reaction pathway for a simple bacterial transposase (carried by the Tn5 transposon) is also shown.Enlarge
The domain organization of the Hermes transposase and the 3D structure of the protein aloneThe Hermes transposase consists of 612 amino acids. On the monomer level, it is a multidomain protein (domains are represented as colored boxes in the schematic on top) organized around a central catalytic core (orange) that is structurally related to E. coli RNase H.Enlarge
Neisserial Iron Import ComplexNeisseria survive in the human host by utilizing surface receptors to pirate iron from human iron binding proteins. Based on our studies, we were able to describe what the Neisserial import complex looks like at the surface of the pathogen. Shown here is the iron transporter TbpA (purple, red glow indicates iron passage), the co-receptor TbpB (purple, top), the human iron binding protein transferrin (orange), periplasmic proteins FbpA (dark green), and TonB (light green).Enlarge
Structure of the TLR3-ECDThis image depicts the structure of the TLR3-ECD. The TLR3-ECD consists of 23 LRRs that form a horseshoe-like solenoid with two capping motifs. The molecule has a surprisingly flat profile. There are 11 visible glycosylation sites. Figure 1 BBA, 2009.Enlarge
Major muscle cell types in the C. elegans adult hermaphrodite.This schematic depicts major muscle cell types in the C. elegans adult hermaphrodite. A lateral view is provided, with anterior to the left and dorsal on top, of the major muscle types of the nematode C. elegans. Enlarge
The transcriptional cascade is shown for embryonically derived bodywall muscle (BWM) cells.The transcriptional cascade is shown for embryonically derived bodywall muscle (BWM) cells. The C. elegans gene name is indicated in lowercase for each transcription factor, and the names of related factors in mammals are in uppercase. The number of BWM cells derived by each part of the process is indicated parenthetically.Enlarge
Images of master myogenic regulatory transcription factor function in C. elegans.Images of master myogenic regulatory transcription factor function in C. elegans are depicted. At left is the wild-type pattern of bodywall muscle development at the 1.5-fold stage of embryogenesis. The image at the right shows the consequences of expressing the master muscle transcription factor HLH-1 in early blastomeres; almost all embryonic cells adopte the bodywall muscle-like fate. Enlarge
Domains of HIV-1 integraseThis image depicts domains of HIV-1 integrase. HIV-1 integrase comprises three structural domains. The central domain is highly conserved among retroviruses, retrotransposons, and many DNA transposons. It contains the active site for polynucleotidyl transfer. The N-terminal domain contains the HHCC motif that binds zinc. The C-terminal domain is less well conserved.Enlarge
Structures of the individual domains of HIV-1 integraseThis image depicts structures of the individual domains of HIV-1 integrase. A major goal is to understand how these domains are organized in complex with viral DNA (intasomes). Current inhibitors of HIV integrase bind to intasomes rather than free integrase proteins. Understanding the mechanism inhibition and the development of resistance requires high-resolution structures of intasomes.Enlarge
HIV-1 intrasomes visualized by atomic force microscopyHIV-1 intasomes are visualized by atomic force microscopy. A tetramer of integrase (white spot) bridges a pair of DNA ends.Enlarge
Condensation of DNA by barrier-to-autointegration factor (BAF)Condensation of DNA by barrier-to-autointegration factor (BAF) is shown. Single DNA molecules are extended by buffer flow and visualized by fluorescence microscopy. At time zero BAF is introduced into the flow cell. The molecules compact into a ball as a result of DNA bridging by BAF. Depicted are (a) a molecule attached to surface at one end only, (b) a molecule attached at both ends, (C) two molecules attached side-by-side “zipper” together, and (d) other examples of molecules attached at one end.Enlarge