Expression of Human RPS17 and RPS23 in E. Coli Bacterial Cells

dc.contributor.advisorZeidan, Quira
dc.contributor.authorBloom, Kaylee
dc.contributor.authorPerera, Senanga
dc.contributor.authorOutmezguine, Daniel
dc.contributor.authorPatel, Tulsi
dc.contributor.authorHunter, Kennedi
dc.contributor.authorKothari, Yashi
dc.contributor.authorGuevara, Ivan
dc.contributor.authorPham, Thong
dc.date.accessioned2024-04-30T13:24:28Z
dc.date.available2024-04-30T13:24:28Z
dc.date.issued2024-04
dc.description.abstractRibosome biogenesis is vital for a cell to make proteins and proceed through the central dogma of molecular biology. Human ribosomal proteins (RPs) RPS17 and RPS23 are protein-encoding genes associated with the formation of ribosomes in cells. Serious diseases are linked to dysfunction of RPS17 and RPS23. Mutations in RPS17 have been linked to Diamond-Blackfan anemia, a rare inherited bone marrow disease that affects red blood cells, leading to anemia. RPS23 protein dysfunction is linked to Hepatocellular carcinoma, a severe form of liver cancer. In this study, RPS17 and RPS23 were cloned and expressed with two different bacterial expression plasmids, pNIC28-Bsa4 and pNH-TrxT, with 100% sequence confirmation. Plasmids were then transformed into BL21 E. coli cells, and IPTG induction was used to express RPS17 and RPS23. SDS-PAGE, followed by Coomassie staining, was conducted to confirm the successful expression of the proteins. Future research will determine how overexpression and posttranslational modifications of RPS17 and RPS23 link to cellular growth and homeostasis.
dc.identifierhttps://doi.org/10.13016/jvht-4f9a
dc.identifier.urihttp://hdl.handle.net/1903/32553
dc.relation.isAvailableAtDigital Repository at the University of Maryland
dc.relation.isAvailableAtUniversity of Maryland (College Park, Md)
dc.relation.isAvailableAtOffice of Undergraduate Research
dc.subjectFirst-Year Innovation and Research Experience
dc.titleExpression of Human RPS17 and RPS23 in E. Coli Bacterial Cells
dc.typeOther
local.equitableAccessSubmissionNo

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