SUMOylation and the predicted assembly of a plant NuRD-like repressor complex

TOPLESS and TOPLESS-RELATED protein are members of a conserved family of plant co-repressors. They act as general co-repressors to promote transcriptional repression. Loss of TOPLESS-mediated repression radically affects development and other central processes. Repression via TOPLESS is dependent on...

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Main Author: Plant, Alastair Robert
Other Authors: Davies, Brendan H.
Published: University of Leeds 2018
Subjects:
570
Online Access:https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.766427
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spelling ndltd-bl.uk-oai-ethos.bl.uk-7664272019-03-05T16:04:28ZSUMOylation and the predicted assembly of a plant NuRD-like repressor complexPlant, Alastair RobertDavies, Brendan H.2018TOPLESS and TOPLESS-RELATED protein are members of a conserved family of plant co-repressors. They act as general co-repressors to promote transcriptional repression. Loss of TOPLESS-mediated repression radically affects development and other central processes. Repression via TOPLESS is dependent on the activity of histone deacetylases, but direct interaction between the two has not been observed, although both TOPLESS and HISTONE DEACETYLASE 19 interact with proteins shared with the animal Nucleosome Remodelling and histone Deacetylation complex. Some interactions between co-repressors and histone deacetylases are dependent on the involvement of SMALL UBIQUITIN-LIKE MODIFIERS. TOPLESS and TOPLESS-RELATED proteins are reported to be SUMOylated. The floral phenotype of loss-of-function tpl-1 mutants is enhanced by the SUMO ligase mutant siz1-2. Abnormal tpl-1 flowers are not seen after crossing tpl-1 mutants with mutants of the SUMO proteases OVERLY TOLERANT TO SALT 1 and 2. Mutations at predicted SUMOylation sites within TOPLESS affect its ability to complement tpl-1 embryonic phenotypes and abolish recovery of a high molecular-weight protein, potentially a TOPLESS-SUMO conjugate. Attempts to co-precipitate SUMOylated TOPLESS and NuRD-associated proteins did not recover an intact complex but provided evidence to support heteromeric interactions between TOPLESS and TOPLESS-RELATED proteins. Additionally, the chromatin regulator SPLAYED was identified as a potential interactor or antagonist. Development of novel topless and topless-related mutant combinations shed light on the functional redundancy of family members and has created a platform for improved complementation assays. Additionally, discovery of an unreported root phenotype in the mutants will allow use of a more quantitative approach to phenotypic scoring. Phylogenetic analysis reveals the absence of a conserved subclade of the TOPLESS family from Arabidopsis with implications for evolutionary and functional comparisons with other species, but suggests long-term conservation of a candidate SUMOylation site. SUMO may be involved in regulating TOPLESS function across plants.570University of Leedshttps://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.766427http://etheses.whiterose.ac.uk/22592/Electronic Thesis or Dissertation
collection NDLTD
sources NDLTD
topic 570
spellingShingle 570
Plant, Alastair Robert
SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
description TOPLESS and TOPLESS-RELATED protein are members of a conserved family of plant co-repressors. They act as general co-repressors to promote transcriptional repression. Loss of TOPLESS-mediated repression radically affects development and other central processes. Repression via TOPLESS is dependent on the activity of histone deacetylases, but direct interaction between the two has not been observed, although both TOPLESS and HISTONE DEACETYLASE 19 interact with proteins shared with the animal Nucleosome Remodelling and histone Deacetylation complex. Some interactions between co-repressors and histone deacetylases are dependent on the involvement of SMALL UBIQUITIN-LIKE MODIFIERS. TOPLESS and TOPLESS-RELATED proteins are reported to be SUMOylated. The floral phenotype of loss-of-function tpl-1 mutants is enhanced by the SUMO ligase mutant siz1-2. Abnormal tpl-1 flowers are not seen after crossing tpl-1 mutants with mutants of the SUMO proteases OVERLY TOLERANT TO SALT 1 and 2. Mutations at predicted SUMOylation sites within TOPLESS affect its ability to complement tpl-1 embryonic phenotypes and abolish recovery of a high molecular-weight protein, potentially a TOPLESS-SUMO conjugate. Attempts to co-precipitate SUMOylated TOPLESS and NuRD-associated proteins did not recover an intact complex but provided evidence to support heteromeric interactions between TOPLESS and TOPLESS-RELATED proteins. Additionally, the chromatin regulator SPLAYED was identified as a potential interactor or antagonist. Development of novel topless and topless-related mutant combinations shed light on the functional redundancy of family members and has created a platform for improved complementation assays. Additionally, discovery of an unreported root phenotype in the mutants will allow use of a more quantitative approach to phenotypic scoring. Phylogenetic analysis reveals the absence of a conserved subclade of the TOPLESS family from Arabidopsis with implications for evolutionary and functional comparisons with other species, but suggests long-term conservation of a candidate SUMOylation site. SUMO may be involved in regulating TOPLESS function across plants.
author2 Davies, Brendan H.
author_facet Davies, Brendan H.
Plant, Alastair Robert
author Plant, Alastair Robert
author_sort Plant, Alastair Robert
title SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
title_short SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
title_full SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
title_fullStr SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
title_full_unstemmed SUMOylation and the predicted assembly of a plant NuRD-like repressor complex
title_sort sumoylation and the predicted assembly of a plant nurd-like repressor complex
publisher University of Leeds
publishDate 2018
url https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.766427
work_keys_str_mv AT plantalastairrobert sumoylationandthepredictedassemblyofaplantnurdlikerepressorcomplex
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