Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation

At variance with the starch-accumulating plants and most of the glycogen-accumulating cyanobacteria, Cyanobacterium sp. CLg1 synthesizes both glycogen and starch. We now report the selection of a starchless mutant of this cyanobacterium that retains wild-type amounts of glycogen. Unlike other mutant...

Descripción completa

Detalles Bibliográficos
Autores: Kadouche, Derifa, Ducatez, Mathieu, Cenci, Ugo, Tirtiaux, Catherine, Suzuki, Eiji, Nakamura, Yasunori, Putaux, Jean Luc, Terrasson, Amandine Dur, Díaz Troya, Sandra, Florencio Bellido, Francisco Javier, Arias, Maria Cecilia, Striebeck, Alexander, Palcic, Monica, Ball, Steven G., Colleoni, Christophe
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/130187
Acceso en línea:https://hdl.handle.net/11441/130187
https://doi.org/10.1104/pp.16.00049
Access Level:acceso abierto
id ES_55bc00421d0f44bbc2f31fbf5e310fac
oai_identifier_str oai:idus.us.es:11441/130187
network_acronym_str ES
network_name_str España
repository_id_str
spelling Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregationKadouche, DerifaDucatez, MathieuCenci, UgoTirtiaux, CatherineSuzuki, EijiNakamura, YasunoriPutaux, Jean LucTerrasson, Amandine DurDíaz Troya, SandraFlorencio Bellido, Francisco JavierArias, Maria CeciliaStriebeck, AlexanderPalcic, MonicaBall, Steven G.Colleoni, ChristopheAt variance with the starch-accumulating plants and most of the glycogen-accumulating cyanobacteria, Cyanobacterium sp. CLg1 synthesizes both glycogen and starch. We now report the selection of a starchless mutant of this cyanobacterium that retains wild-type amounts of glycogen. Unlike other mutants of this type found in plants and cyanobacteria, this mutant proved to be selectively defective for one of the two types of glycogen/starch synthase: GlgA2. This enzyme is phylogenetically related to the previously reported SSIII/SSIV starch synthase that is thought to be involved in starch granule seeding in plants. This suggests that, in addition to the selective polysaccharide debranching demonstrated to be responsible for starch rather than glycogen synthesis, the nature and properties of the elongation enzyme define a novel determinant of starch versus glycogen accumulation. We show that the phylogenies of GlgA2 and of 16S ribosomal RNA display significant congruence. This suggests that this enzyme evolved together with cyanobacteria when they diversified over 2 billion years ago. However, cyanobacteria can be ruled out as direct progenitors of the SSIII/SSIV ancestral gene found in Archaeplastida. Hence, both cyanobacteria and plants recruited similar enzymes independently to perform analogous tasks, further emphasizing the importance of convergent evolution in the appearance of starch from a preexisting glycogen metabolism network.Agence Nationale de la Recherche ANR–BLAN07– 3–186613American Society of Plant BiologistsBioquímica Vegetal y Biología Molecular2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/130187https://doi.org/10.1104/pp.16.00049reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésPlant Physiology, 171 (3), 1879-1892.ANR–BLAN07– 3–186613https://doi.org/10.1104/pp.16.00049info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1301872026-06-17T12:51:07Z
dc.title.none.fl_str_mv Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
title Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
spellingShingle Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
Kadouche, Derifa
title_short Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
title_full Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
title_fullStr Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
title_full_unstemmed Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
title_sort Characterization of function of the GlgA2 glycogen/starch synthase in Cyanobacterium sp. Clg1 highlights convergent evolution of glycogen metabolism into starch granule aggregation
dc.creator.none.fl_str_mv Kadouche, Derifa
Ducatez, Mathieu
Cenci, Ugo
Tirtiaux, Catherine
Suzuki, Eiji
Nakamura, Yasunori
Putaux, Jean Luc
Terrasson, Amandine Dur
Díaz Troya, Sandra
Florencio Bellido, Francisco Javier
Arias, Maria Cecilia
Striebeck, Alexander
Palcic, Monica
Ball, Steven G.
Colleoni, Christophe
author Kadouche, Derifa
author_facet Kadouche, Derifa
Ducatez, Mathieu
Cenci, Ugo
Tirtiaux, Catherine
Suzuki, Eiji
Nakamura, Yasunori
Putaux, Jean Luc
Terrasson, Amandine Dur
Díaz Troya, Sandra
Florencio Bellido, Francisco Javier
Arias, Maria Cecilia
Striebeck, Alexander
Palcic, Monica
Ball, Steven G.
Colleoni, Christophe
author_role author
author2 Ducatez, Mathieu
Cenci, Ugo
Tirtiaux, Catherine
Suzuki, Eiji
Nakamura, Yasunori
Putaux, Jean Luc
Terrasson, Amandine Dur
Díaz Troya, Sandra
Florencio Bellido, Francisco Javier
Arias, Maria Cecilia
Striebeck, Alexander
Palcic, Monica
Ball, Steven G.
Colleoni, Christophe
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
description At variance with the starch-accumulating plants and most of the glycogen-accumulating cyanobacteria, Cyanobacterium sp. CLg1 synthesizes both glycogen and starch. We now report the selection of a starchless mutant of this cyanobacterium that retains wild-type amounts of glycogen. Unlike other mutants of this type found in plants and cyanobacteria, this mutant proved to be selectively defective for one of the two types of glycogen/starch synthase: GlgA2. This enzyme is phylogenetically related to the previously reported SSIII/SSIV starch synthase that is thought to be involved in starch granule seeding in plants. This suggests that, in addition to the selective polysaccharide debranching demonstrated to be responsible for starch rather than glycogen synthesis, the nature and properties of the elongation enzyme define a novel determinant of starch versus glycogen accumulation. We show that the phylogenies of GlgA2 and of 16S ribosomal RNA display significant congruence. This suggests that this enzyme evolved together with cyanobacteria when they diversified over 2 billion years ago. However, cyanobacteria can be ruled out as direct progenitors of the SSIII/SSIV ancestral gene found in Archaeplastida. Hence, both cyanobacteria and plants recruited similar enzymes independently to perform analogous tasks, further emphasizing the importance of convergent evolution in the appearance of starch from a preexisting glycogen metabolism network.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/130187
https://doi.org/10.1104/pp.16.00049
url https://hdl.handle.net/11441/130187
https://doi.org/10.1104/pp.16.00049
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Plant Physiology, 171 (3), 1879-1892.
ANR–BLAN07– 3–186613
https://doi.org/10.1104/pp.16.00049
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society of Plant Biologists
publisher.none.fl_str_mv American Society of Plant Biologists
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869408327991033856
score 15.301603

Similares en LA Referencia