Publication

Molecular interactions within an antagonistic module of protein involved in plant developmental processes

View document

Bibliographic Details
Summary:The protein-protein interactions (PPIs) underlying the interplay between plant transcription factors (TFs) have not been studied in detail; however, understanding their interaction is important to unravel Gene Regulatory Networks. The Antirrhinum majus asymmetric flower development involves the proteins DIVARICATA (DIV), RADIALIAS (RAD) and DIV-and-RAD interacting factor (DRIF) working in the tug-of-war DIV-DRIF-RAD (DDR) regulatory module. It functions as an on/off molecular switch, in which DIV and DRIF can interact in a DNA-binding complex; RAD can sequester the DRIF in the cytoplasm, preventing the establishment of the DIV-DRIF complex. The module has been co-opted into different functions across several species. In Arabidopsis thaliana it is unclear whether the DDR homologous proteins work as a module, despite previous work showing involvement of individual genes in the control of several molecular processes. One of the aims of this work was to characterize the expression of the DDR genes in tissues and conditions in A. thaliana to unveil a possible involvement of the DDR regulatory module during development, as well as in the response to abiotic stresses and in the regulation of hormone signalling. Another aim of the work was to obtain recombinant protein to in the future perform biophysical assays to further characterize the molecular mechanism through which RAD antagonizes the DIV function by establishing a complex with the DRIF protein. Only AmRAD1 was previously expressed and purified. In this work, the conditions for the expression of soluble AmDIV1, MpDIV1, and AtDRIF3 were optimized. The last aim of the work was to determine the amino acid residues that establish PPI between AmRAD and AmDRIF binding through in silico analysis of the AmRAD1 crystal structure and the AmDRIF1 MYB simulated structure. Some AmRAD1 residues potentially involved in PPI were tested through site-directed mutagenesis and by yeast two-hybrid assays. The identified residues were utilized to restrict the simulated models of interaction between the AmRAD1 and AmDRIF1 structures. The results from this work will take us closer to understanding the DDR module by identifying new processes in which it is involved. It will also take us closer to understanding the RAD-DRIF and DIV-DRIF complexes, which may be used to fine tune the module into a system for graded expression, which would allow the regulation of the phenotype associated with the module.
Main Authors:Sousa, Ângela Simone Gonçalves de
Subject:DIV-DRIF-RAD regulatory module Heterologous protein expression Protein-protein interactions Relative gene expression Expressão de proteínas heterólogas Expressão genética relativa Interações proteína-proteína Módulo regulatório DIV-DRIF-RAD
Year:2022
Country:Portugal
Document type:master thesis
Access type:open access
Associated institution:Universidade do Minho
Language:English
Origin:RepositóriUM - Universidade do Minho
_version_ 1866878019590684672
author Sousa, Ângela Simone Gonçalves de
author_facet Sousa, Ângela Simone Gonçalves de
author_role author
contributor_name_str_mv Costa, Maria Manuela Ribeiro
Romão, Célia Maria Valente
Universidade do Minho
country_str PT
creators_json_txt [{\"Person.name\":\"Sousa, Ângela Simone Gonçalves de\"}]
datacite.contributors.contributor.contributorName.fl_str_mv Costa, Maria Manuela Ribeiro
Romão, Célia Maria Valente
Universidade do Minho
datacite.creators.creator.creatorName.fl_str_mv Sousa, Ângela Simone Gonçalves de
datacite.date.Accepted.fl_str_mv 2022-12-20T00:00:00Z
datacite.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_abf2
datacite.subjects.subject.fl_str_mv DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
datacite.titles.title.fl_str_mv Molecular interactions within an antagonistic module of protein involved in plant developmental processes
Interações moleculares num módulo antagonista de proteínas envolvidas em processos de desenvolvimento de plantas
dc.contributor.none.fl_str_mv Costa, Maria Manuela Ribeiro
Romão, Célia Maria Valente
Universidade do Minho
dc.creator.none.fl_str_mv Sousa, Ângela Simone Gonçalves de
dc.date.Accepted.fl_str_mv 2022-12-20T00:00:00Z
dc.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv https://hdl.handle.net/1822/84550
dc.language.none.fl_str_mv eng
dc.rights.cclincense.fl_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.rights.copyright.fl_str_mv closedAccess
dc.subject.none.fl_str_mv DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
dc.title.fl_str_mv Molecular interactions within an antagonistic module of protein involved in plant developmental processes
Interações moleculares num módulo antagonista de proteínas envolvidas em processos de desenvolvimento de plantas
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_bdcc
description The protein-protein interactions (PPIs) underlying the interplay between plant transcription factors (TFs) have not been studied in detail; however, understanding their interaction is important to unravel Gene Regulatory Networks. The Antirrhinum majus asymmetric flower development involves the proteins DIVARICATA (DIV), RADIALIAS (RAD) and DIV-and-RAD interacting factor (DRIF) working in the tug-of-war DIV-DRIF-RAD (DDR) regulatory module. It functions as an on/off molecular switch, in which DIV and DRIF can interact in a DNA-binding complex; RAD can sequester the DRIF in the cytoplasm, preventing the establishment of the DIV-DRIF complex. The module has been co-opted into different functions across several species. In Arabidopsis thaliana it is unclear whether the DDR homologous proteins work as a module, despite previous work showing involvement of individual genes in the control of several molecular processes. One of the aims of this work was to characterize the expression of the DDR genes in tissues and conditions in A. thaliana to unveil a possible involvement of the DDR regulatory module during development, as well as in the response to abiotic stresses and in the regulation of hormone signalling. Another aim of the work was to obtain recombinant protein to in the future perform biophysical assays to further characterize the molecular mechanism through which RAD antagonizes the DIV function by establishing a complex with the DRIF protein. Only AmRAD1 was previously expressed and purified. In this work, the conditions for the expression of soluble AmDIV1, MpDIV1, and AtDRIF3 were optimized. The last aim of the work was to determine the amino acid residues that establish PPI between AmRAD and AmDRIF binding through in silico analysis of the AmRAD1 crystal structure and the AmDRIF1 MYB simulated structure. Some AmRAD1 residues potentially involved in PPI were tested through site-directed mutagenesis and by yeast two-hybrid assays. The identified residues were utilized to restrict the simulated models of interaction between the AmRAD1 and AmDRIF1 structures. The results from this work will take us closer to understanding the DDR module by identifying new processes in which it is involved. It will also take us closer to understanding the RAD-DRIF and DIV-DRIF complexes, which may be used to fine tune the module into a system for graded expression, which would allow the regulation of the phenotype associated with the module.
dirty 0
eu_rights_str_mv openAccess
format masterThesis
fulltext.url.fl_str_mv https://prod-dspace.uminho.pt/bitstreams/da7b77d8-1d1e-4d03-a1a7-e86e1eaa7058/download
id rum_4e403012ff8a87a9fd3d12fa588c2543
identifier.url.fl_str_mv https://hdl.handle.net/1822/84550
instacron_str repositorium
institution Universidade do Minho
instname_str Universidade do Minho
language eng
network_acronym_str rum
network_name_str RepositóriUM - Universidade do Minho
oai_identifier_str oai:repositorium.uminho.pt:1822/84550
organization_str_mv urn:organizationAcronym:repositorium
person_str_mv Sousa, Ângela Simone Gonçalves de
publishDate 2022
reponame_str RepositóriUM - Universidade do Minho
repository_id_str urn:repositoryAcronym:rum
service_str_mv urn:repositoryAcronym:rum
spelling engporThe protein-protein interactions (PPIs) underlying the interplay between plant transcription factors (TFs) have not been studied in detail; however, understanding their interaction is important to unravel Gene Regulatory Networks. The Antirrhinum majus asymmetric flower development involves the proteins DIVARICATA (DIV), RADIALIAS (RAD) and DIV-and-RAD interacting factor (DRIF) working in the tug-of-war DIV-DRIF-RAD (DDR) regulatory module. It functions as an on/off molecular switch, in which DIV and DRIF can interact in a DNA-binding complex; RAD can sequester the DRIF in the cytoplasm, preventing the establishment of the DIV-DRIF complex. The module has been co-opted into different functions across several species. In Arabidopsis thaliana it is unclear whether the DDR homologous proteins work as a module, despite previous work showing involvement of individual genes in the control of several molecular processes. One of the aims of this work was to characterize the expression of the DDR genes in tissues and conditions in A. thaliana to unveil a possible involvement of the DDR regulatory module during development, as well as in the response to abiotic stresses and in the regulation of hormone signalling. Another aim of the work was to obtain recombinant protein to in the future perform biophysical assays to further characterize the molecular mechanism through which RAD antagonizes the DIV function by establishing a complex with the DRIF protein. Only AmRAD1 was previously expressed and purified. In this work, the conditions for the expression of soluble AmDIV1, MpDIV1, and AtDRIF3 were optimized. The last aim of the work was to determine the amino acid residues that establish PPI between AmRAD and AmDRIF binding through in silico analysis of the AmRAD1 crystal structure and the AmDRIF1 MYB simulated structure. Some AmRAD1 residues potentially involved in PPI were tested through site-directed mutagenesis and by yeast two-hybrid assays. The identified residues were utilized to restrict the simulated models of interaction between the AmRAD1 and AmDRIF1 structures. The results from this work will take us closer to understanding the DDR module by identifying new processes in which it is involved. It will also take us closer to understanding the RAD-DRIF and DIV-DRIF complexes, which may be used to fine tune the module into a system for graded expression, which would allow the regulation of the phenotype associated with the module.application/pdfporMolecular interactions within an antagonistic module of protein involved in plant developmental processesAlternativeTitleporInterações moleculares num módulo antagonista de proteínas envolvidas em processos de desenvolvimento de plantasSousa, Ângela Simone Gonçalves deCosta, Maria Manuela RibeiroRomão, Célia Maria ValenteHostingInstitutionOrganizationalUniversidade do Minhoe-mailmailto:repositorium@usdb.uminho.ptrepositorium@usdb.uminho.ptURNurn:tid:2032328102022-12-202022-1010000-01-01T00:00:00Z2022-12-20T00:00:00ZHandlehttps://hdl.handle.net/1822/84550http://purl.org/coar/access_right/c_abf2open accessDIV-DRIF-RAD regulatory moduleHeterologous protein expressionProtein-protein interactionsRelative gene expressionExpressão de proteínas heterólogasExpressão genética relativaInterações proteína-proteínaMódulo regulatório DIV-DRIF-RAD5660779 bytesliteraturehttp://purl.org/coar/resource_type/c_bdccmaster thesis2022-12-20http://creativecommons.org/licenses/by-nc-nd/4.0/closedAccesshttp://purl.org/coar/access_right/c_abf2application/pdffulltexthttps://prod-dspace.uminho.pt/bitstreams/da7b77d8-1d1e-4d03-a1a7-e86e1eaa7058/download
spellingShingle Molecular interactions within an antagonistic module of protein involved in plant developmental processes
Sousa, Ângela Simone Gonçalves de
DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
status SINGLETON
subject.fl_str_mv DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
title Molecular interactions within an antagonistic module of protein involved in plant developmental processes
title_full Molecular interactions within an antagonistic module of protein involved in plant developmental processes
title_fullStr Molecular interactions within an antagonistic module of protein involved in plant developmental processes
title_full_unstemmed Molecular interactions within an antagonistic module of protein involved in plant developmental processes
title_short Molecular interactions within an antagonistic module of protein involved in plant developmental processes
title_sort Molecular interactions within an antagonistic module of protein involved in plant developmental processes
topic DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
topic_facet DIV-DRIF-RAD regulatory module
Heterologous protein expression
Protein-protein interactions
Relative gene expression
Expressão de proteínas heterólogas
Expressão genética relativa
Interações proteína-proteína
Módulo regulatório DIV-DRIF-RAD
url https://hdl.handle.net/1822/84550
visible 1