Skip to Main content Skip to Navigation
Theses

Caractérisation biochimique et structurale des RNases P et MRP chez la levure Saccharomyces cerevisiae

Abstract : Ribonuclease P (RNase P) is an endoribonuclease that cleaves the 5'-leader sequence of pre-tRNAs. RNase P is conserved between all taxonomic kingdoms and consists of a catalytic RNA subunit and protein components of variable size, from one protein in bacteria to 5 proteins in archae and at least 9 proteins in eukaryotic cells. In addition to RNase P, eukaryotes possess the RNase MRP which has a related RNA core and shares 8 proteins subunits with RNase P but with its own substrate specificity. Here, we propose an original method to purify specifically RNase P and RNase MRP from S. cerevisiae. Using electron microscopy and image processing, we solved the first structure of these two holoenzymes at a resolution of about 1.5 nm. We showed that eukaryotic RNase P and RNase MRP have a modular architecture, where proteins stabilize the RNA fold and contribute to cavities, channels and chambers between the modules.Structural features are located at strategic positions for substrate recognition by shape and coordination of the cleaved-off sequence.
Document type :
Theses
Complete list of metadatas

https://tel.archives-ouvertes.fr/tel-00804257
Contributor : Abes Star :  Contact
Submitted on : Monday, March 25, 2013 - 11:37:32 AM
Last modification on : Thursday, April 26, 2018 - 3:18:34 AM
Long-term archiving on: : Sunday, April 2, 2017 - 7:49:54 PM

File

Batisse_Claire_2013_ED414.pdf
Version validated by the jury (STAR)

Identifiers

  • HAL Id : tel-00804257, version 1

Collections

Citation

Claire Batisse. Caractérisation biochimique et structurale des RNases P et MRP chez la levure Saccharomyces cerevisiae. Sciences agricoles. Université de Strasbourg, 2013. Français. ⟨NNT : 2013STRAJ001⟩. ⟨tel-00804257⟩

Share

Metrics

Record views

546

Files downloads

797