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Full-Text Articles in Molecular Biology

Elucidating Nucleic Acid Binding Properties Of Polycomb Repressive Complex 2, Richard D. Paucek Jan 2017

Elucidating Nucleic Acid Binding Properties Of Polycomb Repressive Complex 2, Richard D. Paucek

Undergraduate Honors Theses

Polycomb Repressive Complex 2 (PRC2) is a histone methyltransferase that specifically deposits mono-, di-, and tri-methylation marks onto chromatin. This activity triggers epigenetic silencing, a process critical for cell differentiation and maintenance of cellular identity. In mammalian cells, how PRC2 is recruited to target sites is unknown, but it is speculated that RNA, histone modifications, nucleosome architecture, and DNA elements all possess direct or indirect recruitment and regulatory roles. However, the relative binding affinity of PRC2 for these diverse biological substrates remains poorly understood. In the present study, the binding affinity of PRC2 for various RNAs and nucleosomes were tested ...


Single Human Cells Use Transcriptional Mechanisms To Compensate For Differences In Cell Size And Dna Content, Olivia Padovan-Merhar Jan 2015

Single Human Cells Use Transcriptional Mechanisms To Compensate For Differences In Cell Size And Dna Content, Olivia Padovan-Merhar

Publicly Accessible Penn Dissertations

Human cells are dynamic: they grow, replicate their genetic information (DNA), and divide. Clonal populations of cells can display marked heterogeneity in size, leading to significant variability in the ratio of DNA to cellular volume. Despite this variability, cells must maintain a constant concentration of RNA and protein, produced from DNA, to ensure proper functionality. How do larger cells produce more output from the same amount of DNA? How do cells that have replicated their DNA prior to cellular division produce the same output as before? Using RNA fluorescence in situ hybridization (RNA FISH), we visualize and count individual RNA ...


Identification Of Molecular Determinants That Shift Co- And Post-Translational N-Glycosylation Kinetics In Type I Transmembrane Peptides: A Dissertation, Heidi L. H. Malaby Apr 2014

Identification Of Molecular Determinants That Shift Co- And Post-Translational N-Glycosylation Kinetics In Type I Transmembrane Peptides: A Dissertation, Heidi L. H. Malaby

GSBS Dissertations and Theses

Asparagine (N)-linked glycosylation occurs on 90% of membrane and secretory proteins and drives folding and trafficking along the secretory pathway. The N-glycan can be attached to an N-X-T/S-Y (X,Y ≠ P) consensus site by one of two oligosaccharyltransferase (OST) STT3 enzymatic isoforms either during protein translation (co-translational) or after protein translation has completed (post-translational). While co-translational N-glycosylation is both rapid and efficient, post-translational N-glycosylation occurs on a much slower time scale and, due to competition with protein degradation and forward trafficking, could be detrimental to the success of a peptide heavily reliant on post-translational N-glycosylation. In evidence, mutations ...