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Search Results: 1 - 10 of 1758 matches for " Liza Larsen "
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Two-hybrid analysis of Ty3 capsid subdomain interactions
Min Zhang, Liza SZ Larsen, Becky Irwin, Virginia Bilanchone, Suzanne Sandmeyer
Mobile DNA , 2010, DOI: 10.1186/1759-8753-1-14
Abstract: Two-hybrid analysis was used to understand the interactions that contribute to particle assembly. Gag3 interacted with itself as predicted based on its role as the major structural protein. The N-terminal subdomain (NTD) of the capsid was able to interact with itself and with the C-terminal subdomain (CTD) of the capsid, but interacted less well with intact Gag3. Mutations previously shown to block particle assembly disrupted Gag3 interactions more than subdomain interactions.The findings that the NTD interacts with itself and with the CTD are consistent with previous modeling and a role similar to that of the capsid in retrovirus particle structure. These results are consistent with a model in which the Gag3-Gag3 interactions that initiate assembly differ from the subdomain interactions that potentially underlie particle stability.The Ty3 retrotransposon in budding yeast forms virus-like particles (VLPs) comprised of precursor Gag3 and Gag3-Pol3 polyproteins [1,2]. Previous alanine-scanning mutagenesis indicated that the N-terminal domain (NTD) of the structural polyprotein Gag3 plays an important role in VLP formation [3]. During maturation, Gag3 is processed into 24 kDa capsid (CA), 27 kDa CA-spacer (SP), 3 kDa SP, and 7 kDa nucleocapsid (NC) protein by the Ty3 protease. Unlike most retrovirus cores, these cytoplasmic particles remain stable after proteolytic maturation.Two-hybrid analysis [4] was used to better understand the contributions of Gag3 subdomains to formation and stability of the Ty3 VLP. Fusions of Gag3 and derivatives to the C-terminus of the Gal4-BD tagged with c-Myc were expressed from the high-copy, TRP1-marked pGBK vector (Clontech, Palo Alto, CA, USA). Fusions of Gag3 and derivatives to the C-terminus of the Gal4-AD tagged with HA were expressed from the LEU2-marked high-copy plasmid pGAD T7 (pGAD). These fusions were constructed by amplifying the appropriate regions from Ty3 Gag3 subclones in pGEM (Invitrogen, Carlsbad, CA, USA) using polymer
Directed DNA Shuffling of Retrovirus and Retrotransposon Integrase Protein Domains
Xiaojie Qi, Edwin Vargas, Liza Larsen, Whitney Knapp, G. Wesley Hatfield, Richard Lathrop, Suzanne Sandmeyer
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0063957
Abstract: Chimeric proteins are used to study protein domain functions and to recombine protein domains for novel or optimal functions. We used a library of chimeric integrase proteins to study DNA integration specificity. The library was constructed using a directed shuffling method that we adapted from fusion PCR. This method easily and accurately shuffles multiple DNA gene sequences simultaneously at specific base-pair positions, such as protein domain boundaries. It produced all 27 properly-ordered combinations of the amino-terminal, catalytic core, and carboxyl-terminal domains of the integrase gene from human immunodeficiency virus, prototype foamy virus, and Saccharomyces cerevisiae retrotransposon Ty3. Retrotransposons can display dramatic position-specific integration specificity compared to retroviruses. The yeast retrotransposon Ty3 integrase interacts with RNA polymerase III transcription factors to target integration at the transcription initiation site. In vitro assays of the native and chimeric proteins showed that human immunodeficiency virus integrase was active with heterologous substrates, whereas prototype foamy virus and Ty3 integrases were not. This observation was consistent with a lower substrate specificity for human immunodeficiency virus integrase than for other retrovirus integrases. All eight chimeras containing the Ty3 integrase carboxyl-terminal domain, a candidate targeting domain, failed to target strand transfer in the presence of the targeting protein, suggesting that multiple domains of the Ty3 integrase cooperate in this function.
Regenerating Zebrafish Hearts Reveal the Molecular Agents of Repair
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040281
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Smashing Protein Complex Ions to Bits Reveals Their Structural Organization
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040287
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Cultivating Bacteria's Taste for Toxic Waste
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040282
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Bacterial Fimbriae Designed to Stay with the Flow
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040314
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Master Proteins Dictate Retinal Differentiation Timetable
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040293
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Evolution of Neonatal Imitation
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040311
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Classic Illusion Sheds New Light on the Neural Site of Tactile Perception
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040096
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Genetic Evidence that Humans Have Pushed Orang-utans to the Brink of Extinction
Liza Gross
PLOS Biology , 2012, DOI: 10.1371/journal.pbio.0040057
Abstract:
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