Structural studies on ASAP, a conserved, EJC-associated complex [Elektronische Ressource] / Andrea Giovanni Murachelli. Betreuer: Elena Conti
146 pages
English

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Structural studies on ASAP, a conserved, EJC-associated complex [Elektronische Ressource] / Andrea Giovanni Murachelli. Betreuer: Elena Conti

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146 pages
English
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Description

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Informations

Publié par
Publié le 01 janvier 2011
Nombre de lectures 15
Langue English
Poids de l'ouvrage 16 Mo

Extrait

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ASAP (Apoptosis and Splicing Associated Protein complex) is a protein complex
comprising three members: Acinus, SAP18 and RNPS1. In multicellular eukaryotes, ASAP is
found in spliceosome purifications and is known to interact with the exon junction complex
(EJC), a protein complex with diverse functions in splicing, mRNA localisation and nonsense
mediated decay. These associations suggest that ASAP might play an as yet unknown role in
mRNA maturation. To shed light on this issue, in this thesis I characterised the minimal core
of ASAP and showed that Acinus interacts with its partners through a novel domain, the
ABM (ASAP binding motif). I solved the crystallographic structure of the core ASAP and
used the structural knowledge to identify ABMs in other eukaryotic proteins. Additionally, I
solved two crystallographic structures of SAP18. This allowed the identification of a con-
served interaction surface on the protein, which might mediate contacts with evolutionary
conserved partners. Based on the structural data presented here, I suggest new avenues of re-
search that might shed light on the cellular roles of SAP18 and ASAP.
1

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