Regulation of sumoylation: The identification of ZNF451 as a SUMO E3 ligase and the consequences of sumoylation on the enzymatic activity of the ubiquitin E3 ligase, RNF4
Başlık çevirisi mevcut değil.
- Tez No: 402927
- Danışmanlar: DR. ANDREA PICHLER
- Tez Türü: Doktora
- Konular: Biyoloji, Biology
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 2014
- Dil: İngilizce
- Üniversite: Albert-Ludwigs-Universität Freiburg im Breisgau
- Enstitü: Yurtdışı Enstitü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 145
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Özet (Çeviri)
Post-translational modifications (PTMs) are a quick and efficient means of changing the function of target proteins compared to the energetically expensive and relatively slow de novo protein synthesis. PTM modifiers can be covalently attached to the target protein in in the form of small proteins such as ubiquitin and SUMO (small ubiquitin-like modifier). Ubiquitin conjugation (ubiquitination) and SUMO conjugation (sumoylation) affects diverse cellular pathways such as DNA repair, transcription, genomic stability and proteasomal degradation. Ubiquitin and SUMO are attached to target proteins in a similar series of reactions involving a modifier-specific E1 activating enzyme, an E2 conjugating enzyme and an E3 ligase. To date, only a few SUMO E3 ligases have been identified compared to numerous reported SUMO substrates. Since sumoylation is a tightly regulated and target-specific modification, the small number of SUMO E3 ligases so far identified implies that there are more E3 ligases yet to be discovered. In the work presented in this thesis, I identify ZNF451, a PML body-associated transcriptional corepressor in TGF-β signalling, as a novel mammalian SUMO E3 ligase. In addition, biochemical analysis demonstrates that ZNF451 has a preference for SUMO2. Previously, our group had shown that the sumoylation of Ubc9, the only E2 enzyme of the sumoylation pathway, regulates its target discrimination. Later, the ubiquitin E3 ligase, RNF4 [(Really Interesting New Gene) finger protein 4], was identified as a novel substrate for sumoylated-Ubc9 in our lab. RNF4 belongs to a special class of ubiquitin E3 ligases, which recognize and ubiquitinate polysumoylated proteins. The in vitro studies presented here provide the first biochemical indication that the enzymatic activity of RNF4 is regulated by sumoylation. In addition, a sumoylation site was verified and a new sumoylation was discovered by mass spectrometric analysis. Termed a SUMO-targeted ubiquitin ligase (STUbL), RNF4 offers a unique example to investigate the SUMOubiquitin crosstalk at the level of a single protein since sumoylation influences its enzymatic activity.
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