106 resultados para DeMaat, Gwen


Relevância:

10.00% 10.00%

Publicador:

Resumo:

Typical general transcription factors, such as TATA binding protein and TFII B, have not yet been identified in any member of the Trypanosomatidae family of parasitic protozoa. Interestingly, mRNA coding genes do not appear to have discrete transcriptional start sites, although in most cases they require an RNA polymerase that has the biochemical properties of eukaryotic RNA polymerase II. A discrete transcription initiation site may not be necessary for mRNA synthesis since the sequences upstream of each transcribed coding region are trimmed from the nascent transcript when a short m7G-capped RNA is added during mRNA maturation. This short 39 nt m7G-capped RNA, the spliced leader (SL) sequence, is expressed as an ∼100 nt long RNA from a set of reiterated, though independently transcribed, genes in the trypanosome genome. Punctuation of the 5′ end of mRNAs by a m7G cap-containing spliced leader is a developing theme in the lower eukaryotic world; organisms as diverse as Euglena and nematode worms, including Caenorhabditis elegans, utilize SL RNA in their mRNA maturation programs. Towards understanding the coordination of SL RNA and mRNA expression in trypanosomes, we have begun by characterizing SL RNA gene expression in the model trypanosome Leptomonas seymouri. Using a homologous in vitro transcription system, we demonstrate in this study that the SL RNA is transcribed by RNA polymerase II. During SL RNA transcription, accurate initiation is determined by an initiator element with a loose consensus of CYAC/AYR(+1). This element, as well as two additional basal promoter elements, is divergent in sequence from the basal transcription elements seen in other eukaryotic gene promoters. We show here that the in vitro transcription extract contains a binding activity that is specific for the initiator element and thus may participate in recruiting RNA polymerase II to the SL RNA gene promoter.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

A collection of fifteen poems is presented that deals with mental fragmentation and the fluidity of meaning. The work is a contribution to contemporary poetry, and it cannot be aligned with a specific movement, neither is it a criticism of any previous works; it is generally reflective of postmodernist poetry and postmodern psychology.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Mode of access: Internet.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

"First published in 1916."

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Includes index.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Each v. has also special t.-p.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Mode of access: Internet.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

l-r: Gwen Dew, UM captain Bennie Oosterbaan, OSU captain Theodore Meyer, Miss Tallant, during opening ceremony at stadium dedication.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Back Row: dead coach Jim Richardson, Carloyn Kennedy, Stephanie Liebner, Susie Rabiah, Jennifer Jackson, Molly Hegarty, Amy Honig, Minoo Gupta, Jennifer Eck, Chrissi Rawak, Michelle Swix, Liz Kowal

Middle Row: Julie Schnorberger, Whitney Scherer, Sharon Colombo, Ann Colloton, Jill Oviatt, Kirsten Hirsch, Heather Rose, Margie Stoll, Brenna Tymko, Tammy Nedell, Gwen DeMatt, diving coach Dick Kimball

Front Row: asst. coach Kara McGrath, Julie Geyer, Paula Colombo, Lisa Anderson, Amy Hansen, Stacy Peshkopia, Stacie Fruth, Margaret Huson, Jen Love, Leigh Ann Blessing, Valerie Lupa

Relevância:

10.00% 10.00%

Publicador:

Resumo:

l-r: Gwen Dew, UM captain Bennie Oosterbaan, OSU captain Theodore Meyer, Miss Tallant, during opening ceremony at Michigan Stadium dedication.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Concert Program

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Discovering the function of an unknown protein, particularly one with neither structural nor functional correlates, is a daunting task. Interaction analyses determine binding partners, whereas DNA transfection, either transient or stable, leads to intracellular expression, though not necessarily at physiologically relevant levels. In theory, direct intracellular protein delivery (protein transduction) provides a conceptually simpler alternative, but in practice the approach is problematic. Domains such as HIV TAT protein are valuable, but their effectiveness is protein specific. Similarly, the delivery of intact proteins via endocytic pathways (e.g. using liposomes) is problematic for functional analysis because of the potential for protein degradation in the endosomes/lysosomes. Consequently, recent reports that microspheres can deliver bio-cargoes into cells via a non-endocytic, energy-independent pathway offer an exciting and promising alternative for in vitro delivery of functional protein. In order for such promise to be fully exploited, microspheres are required that (i) are stably linked to proteins, (ii) can deliver those proteins with good efficiency, (iii) release functional protein once inside the cells, and (iv) permit concomitant tracking. Herein, we report the application of microspheres to successfully address all of these criteria simultaneously, for the first time. After cellular uptake, protein release was autocatalyzed by the reducing cytoplasmic environment. Outside of cells, the covalent microsphere-protein linkage was stable for ≥90 h at 37°C. Using conservative methods of estimation, 74.3% ± 5.6% of cells were shown to take up these microspheres after 24 h of incubation, with the whole process of delivery and intracellular protein release occurring within 36 h. Intended for in vitro functional protein research, this approach will enable study of the consequences of protein delivery at physiologically relevant levels, without recourse to nucleic acids, and offers a useful alternative to commercial protein transfection reagents such as Chariot™. We also provide clear immunostaining evidence to resolve residual controversy surrounding FACS-based assessment of microsphere uptake. © 2014 by The American Society for Biochemistry and Molecular Biology Inc.

Relevância:

10.00% 10.00%

Publicador:

Resumo:

Polymer-peptide conjugates (also known as biohy-brids) are attracting considerable attention as injectable materials owing to the self-assembling behavior of the peptide and the ability to control the material properties using the polymer component. To this end, a simple method for preparing poly(ethylene oxide)-oligophenylalanine polymer-peptide conjugates (mPEOm-F n-OEt) using isobutylchloroformate as the activating reagent has been identified and developed. The synthetic approach reported employs an industrially viable route to produce conjugates with high yield and purity. Moreover, the approach allows judicious selection of the precursor building blocks to produce libraries of polymer-peptide conjugates with complete control over the molecular composition. Control over the molecular make-up of the conjugates allows fine control of the physicochemical properties, which will be exploited in future studies into the prominent self-assembling behavior of such materials. © 2013 Wiley Periodicals, Inc.