The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development
Aspergillus nidulans asexual sporulation (conidiation) is triggered by different environmental signals and involves the differentiation of specialized structures called conidiophores. The elimination of genes flbA-E, fluG and tmpA results in a fluffy phenotype characterized by delayed conidiophore d...
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doaj-738800db37a7409cbf3f3414a654c3732020-11-24T23:06:02ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-03-01710.3389/fmicb.2016.00353182566The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual DevelopmentJesus eAguirre0Gabriela eSoid-Raggi1Olivia eSánchez2Jose Luis eRamos-Balderas3Instituto de Fisiologia Celular, UNAMInstituto de Fisiologia Celular, UNAMInstituto de Fisiologia Celular, UNAMInstituto de Fisiologia Celular, UNAMAspergillus nidulans asexual sporulation (conidiation) is triggered by different environmental signals and involves the differentiation of specialized structures called conidiophores. The elimination of genes flbA-E, fluG and tmpA results in a fluffy phenotype characterized by delayed conidiophore development and decreased expression of the conidiation essential gene brlA. While flbA-E encode regulatory proteins, fluG and tmpA encode enzymes involved in the biosynthesis of independent signals needed for normal conidiation. Here we identify afeA and tmpB as new genes encoding members the adenylate-forming enzyme superfamily, whose inactivation cause different fluffy phenotypes and decreased conidiation and brlA expression. AfeA is most similar to unknown function coumarate ligase-like (4CL-Lk) enzymes and consistent with this, a K544N active site modification eliminates AfeA function. TmpB, identified previously as a larger homolog of the oxidoreductase TmpA, contains a NRPS-type adenylation domain. A high degree of synteny in the afeA-tmpA and tmpB regions in the Aspergilli suggests that these genes are part of conserved gene clusters. afeA, tmpA and tmpB double and triple mutant analysis as well as afeA overexpression experiments indicate that TmpA and AfeA act in the same conidiation pathway, with TmpB acting in a different pathway. Fluorescent protein tagging shows that functional versions of AfeA are localized in organelle-type lipid bodies and the plasma membrane, while TmpA and TmpB are localized at the plasma membrane. We propose that AfeA participates in the biosynthesis of an acylated compound, either a p-cuomaryl type or a fatty acid compound, which might be oxidized by TmpA and/or TmpB, while TmpB adenylation domain would be involved in the activation of a hydrophobic amino acid, which in turn would be oxidized by the TmpB oxidoreductase domain. Both, AfeA-TmpA and TmpB signals are involved in self-communication and reproduction in A. nidulans.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.00353/fullsecondary metabolismchemical signalconidiationNRPS“fluffy” mutantsAMP-binding protein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jesus eAguirre Gabriela eSoid-Raggi Olivia eSánchez Jose Luis eRamos-Balderas |
spellingShingle |
Jesus eAguirre Gabriela eSoid-Raggi Olivia eSánchez Jose Luis eRamos-Balderas The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development Frontiers in Microbiology secondary metabolism chemical signal conidiation NRPS “fluffy” mutants AMP-binding protein |
author_facet |
Jesus eAguirre Gabriela eSoid-Raggi Olivia eSánchez Jose Luis eRamos-Balderas |
author_sort |
Jesus eAguirre |
title |
The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development |
title_short |
The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development |
title_full |
The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development |
title_fullStr |
The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development |
title_full_unstemmed |
The Adenylate-Forming Enzymes AfeA And TmpB Are Involved In Aspergillus nidulans Self-Communication During Asexual Development |
title_sort |
adenylate-forming enzymes afea and tmpb are involved in aspergillus nidulans self-communication during asexual development |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Microbiology |
issn |
1664-302X |
publishDate |
2016-03-01 |
description |
Aspergillus nidulans asexual sporulation (conidiation) is triggered by different environmental signals and involves the differentiation of specialized structures called conidiophores. The elimination of genes flbA-E, fluG and tmpA results in a fluffy phenotype characterized by delayed conidiophore development and decreased expression of the conidiation essential gene brlA. While flbA-E encode regulatory proteins, fluG and tmpA encode enzymes involved in the biosynthesis of independent signals needed for normal conidiation. Here we identify afeA and tmpB as new genes encoding members the adenylate-forming enzyme superfamily, whose inactivation cause different fluffy phenotypes and decreased conidiation and brlA expression. AfeA is most similar to unknown function coumarate ligase-like (4CL-Lk) enzymes and consistent with this, a K544N active site modification eliminates AfeA function. TmpB, identified previously as a larger homolog of the oxidoreductase TmpA, contains a NRPS-type adenylation domain. A high degree of synteny in the afeA-tmpA and tmpB regions in the Aspergilli suggests that these genes are part of conserved gene clusters. afeA, tmpA and tmpB double and triple mutant analysis as well as afeA overexpression experiments indicate that TmpA and AfeA act in the same conidiation pathway, with TmpB acting in a different pathway. Fluorescent protein tagging shows that functional versions of AfeA are localized in organelle-type lipid bodies and the plasma membrane, while TmpA and TmpB are localized at the plasma membrane. We propose that AfeA participates in the biosynthesis of an acylated compound, either a p-cuomaryl type or a fatty acid compound, which might be oxidized by TmpA and/or TmpB, while TmpB adenylation domain would be involved in the activation of a hydrophobic amino acid, which in turn would be oxidized by the TmpB oxidoreductase domain. Both, AfeA-TmpA and TmpB signals are involved in self-communication and reproduction in A. nidulans. |
topic |
secondary metabolism chemical signal conidiation NRPS “fluffy” mutants AMP-binding protein |
url |
http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.00353/full |
work_keys_str_mv |
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