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Determining the oligomeric structure of PARN
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2012 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Poly(A)-specific ribonuclease (PARN) is a deadenylase that degrades the poly(A) tail of eukaryotic mRNA. PARN also interacts with the 5’-cap structure of the mRNA. The binding of the cap structure enhances the deadenylation rate. PARN has previously been described as a dimer. We have studied PARN with size exclusion chromatography to investigate the oligomeric composition and revealed oligomeric compositions of PARN that are larger than dimeric PARN. Deadenylation assays have been used to measure the cap stimulated activity of PARN. The deadenylation assays showed that the cap stimulated activity of PARN correlated with the abundance of oligomers corresponding in size to tetrameric PARN. We present a model for tetrameric PARN and propose a mechanistic model for how the cap stimulates PARN mediated deadenylation.

Place, publisher, year, edition, pages
2012. , 31 p.
Series
UPTEC X, 11 048
Keyword [en]
Poly(A)-specific ribonuclease (PARN), deadenylation, mRNA metabolism, cap stimulation, oligomerization
National Category
Cell Biology
Identifiers
URN: urn:nbn:se:uu:diva-167233OAI: oai:DiVA.org:uu-167233DiVA: diva2:482333
Educational program
Molecular Biotechnology Engineering Programme
Presentation
2011-12-15, BMC B7:111, Husargatan 3, Uppsala, 13:15 (Swedish)
Uppsok
Technology
Supervisors
Examiners
Available from: 2012-06-19 Created: 2012-01-23 Last updated: 2012-06-19Bibliographically approved

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CiteExportLink to record
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Citation style
  • apa
  • ieee
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