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Global architecture of human poly(A)-specific ribonuclease by atomic force microscopy in liquid and dynamic light scattering
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2011 (English)In: Biophysical Chemistry, ISSN 0301-4622, E-ISSN 1873-4200, Vol. 158, no 2-3, 141-149 p.Article in journal (Refereed) Published
Abstract [en]

Deadenylation is the initial and often rate-limiting step in the main pathways of eukaryotic mRNA decay. Poly (A)-specific ribonuclease (PARN) is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails. Structural and functional studies have shown that human PARN is composed of at least three functional domains, i.e. the catalytic nuclease domain and two RNA binding domains, the R3H and the RNA recognition motif (RRM), respectively. However, the complete structure of the full length protein is still unknown. We have investigated the global architecture of human PARN by atomic force microscopy (AFM) imaging in buffered milieu and report for the first time the dimensions of the full length protein at subnanometer resolution. The AFM images of single PARN molecules reveal compact ellipsoidal dimers (10.9 x 7.6 x 4.6 nm). The dimeric form of PARN was confirmed by dynamic light scattering (DLS) measurements that rendered a molecular weight of 161 kDa, in accordance with previous crystal structures of PARN fragments showing a dimeric composition. We discuss a putative internal arrangement of three functional domains within the full length PARN dimer.

Place, publisher, year, edition, pages
2011. Vol. 158, no 2-3, 141-149 p.
Keyword [en]
Atomic force microscopy (AFM), Dynamic light scattering (DLS), mRNA decay, Deadenylation, Poly(A)-specific ribonuclease (PARN), RNA recognition motif (RRM)
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-158146DOI: 10.1016/j.bpc.2011.06.010ISI: 000293673900008OAI: oai:DiVA.org:uu-158146DiVA: diva2:438867
Available from: 2011-09-05 Created: 2011-09-01 Last updated: 2011-09-05Bibliographically approved

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