Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles

Retinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa protein shown to play a role in 3'- polyadenylation of mRNA transcripts, as well as to function as an E3 ligase catalysing ubiquitination of cancer-associated proteins. RBBP6 has been previously reported to localise to nuclear speckles, w...

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Main Author: Mlaza, Mihlali
Other Authors: Pugh, David J.R.
Language:en
Published: University of the Western Cape 2018
Subjects:
Online Access:http://hdl.handle.net/11394/6200
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spelling ndltd-netd.ac.za-oai-union.ndltd.org-uwc-oai-etd.uwc.ac.za-11394-62002018-08-08T04:42:14Z Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles Mlaza, Mihlali Pugh, David J.R. RBBP6 DWNN domain Protein localisation Site-directed mutagenesis Nuclear speckles Retinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa protein shown to play a role in 3'- polyadenylation of mRNA transcripts, as well as to function as an E3 ligase catalysing ubiquitination of cancer-associated proteins. RBBP6 has been previously reported to localise to nuclear speckles, which are thought to play a role in mRNA splicing, presumably as a result of its RS domain, which is known to target mRNA splicing factors to nuclear speckles. However recent studies in our laboratory have shown that isoform 3 of RBBP6, consisting mainly of the DWNN domain, also localises to speckles in resting cells, but more strongly in cells subjected to various stresses, suggesting that the DWNN domain may be the speckle-targeting domain. Magister Scientiae - MSc (Biotechnology) 2018-08-06T12:29:23Z 2018-08-06T12:29:23Z 2018 http://hdl.handle.net/11394/6200 en University of the Western Cape University of the Western Cape
collection NDLTD
language en
sources NDLTD
topic RBBP6
DWNN domain
Protein localisation
Site-directed mutagenesis
Nuclear speckles
spellingShingle RBBP6
DWNN domain
Protein localisation
Site-directed mutagenesis
Nuclear speckles
Mlaza, Mihlali
Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
description Retinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa protein shown to play a role in 3'- polyadenylation of mRNA transcripts, as well as to function as an E3 ligase catalysing ubiquitination of cancer-associated proteins. RBBP6 has been previously reported to localise to nuclear speckles, which are thought to play a role in mRNA splicing, presumably as a result of its RS domain, which is known to target mRNA splicing factors to nuclear speckles. However recent studies in our laboratory have shown that isoform 3 of RBBP6, consisting mainly of the DWNN domain, also localises to speckles in resting cells, but more strongly in cells subjected to various stresses, suggesting that the DWNN domain may be the speckle-targeting domain. === Magister Scientiae - MSc (Biotechnology)
author2 Pugh, David J.R.
author_facet Pugh, David J.R.
Mlaza, Mihlali
author Mlaza, Mihlali
author_sort Mlaza, Mihlali
title Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
title_short Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
title_full Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
title_fullStr Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
title_full_unstemmed Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
title_sort investigation of the role of the ubiquitin-like dwnn domain in targeting retinoblastoma binding protein 6 to nuclear speckles
publisher University of the Western Cape
publishDate 2018
url http://hdl.handle.net/11394/6200
work_keys_str_mv AT mlazamihlali investigationoftheroleoftheubiquitinlikedwnndomainintargetingretinoblastomabindingprotein6tonuclearspeckles
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