Cargando…
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A spergillus nidulans
A spergillus nidulans kdmA encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and p...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949671/ https://www.ncbi.nlm.nih.gov/pubmed/25712266 http://dx.doi.org/10.1111/mmi.12977 |
_version_ | 1782443472112844800 |
---|---|
author | Gacek‐Matthews, Agnieszka Noble, Luke M. Gruber, Clemens Berger, Harald Sulyok, Michael Marcos, Ana T. Strauss, Joseph Andrianopoulos, Alex |
author_facet | Gacek‐Matthews, Agnieszka Noble, Luke M. Gruber, Clemens Berger, Harald Sulyok, Michael Marcos, Ana T. Strauss, Joseph Andrianopoulos, Alex |
author_sort | Gacek‐Matthews, Agnieszka |
collection | PubMed |
description | A spergillus nidulans kdmA encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and plays a prominent role in gene expression and chromosome structure in many species. Mass spectrometry mapping of A . nidulans histones revealed that around 3% of bulk histone H3 carried trimethylated H3K9 (H3K9me3) but more than 90% of histones carried either H3K36me2 or H3K36me3. KdmA functions as H3K36me3 demethylase and has roles in transcriptional regulation. Genetic manipulation of KdmA levels is tolerated without obvious effect in most conditions, but strong phenotypes are evident under various conditions of stress. Transcriptome analysis revealed that – in submerged early and late cultures – between 25% and 30% of the genome is under KdmA influence respectively. Transcriptional imbalance in the kdm A deletion mutant may contribute to the lethal phenotype observed upon exposure of mutant cells to low‐density visible light on solid medium. Although KdmA acts as transcriptional co‐repressor of primary metabolism genes, it is required for full expression of several genes involved in biosynthesis of secondary metabolites. |
format | Online Article Text |
id | pubmed-4949671 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49496712016-07-28 KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A spergillus nidulans Gacek‐Matthews, Agnieszka Noble, Luke M. Gruber, Clemens Berger, Harald Sulyok, Michael Marcos, Ana T. Strauss, Joseph Andrianopoulos, Alex Mol Microbiol Research Articles A spergillus nidulans kdmA encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and plays a prominent role in gene expression and chromosome structure in many species. Mass spectrometry mapping of A . nidulans histones revealed that around 3% of bulk histone H3 carried trimethylated H3K9 (H3K9me3) but more than 90% of histones carried either H3K36me2 or H3K36me3. KdmA functions as H3K36me3 demethylase and has roles in transcriptional regulation. Genetic manipulation of KdmA levels is tolerated without obvious effect in most conditions, but strong phenotypes are evident under various conditions of stress. Transcriptome analysis revealed that – in submerged early and late cultures – between 25% and 30% of the genome is under KdmA influence respectively. Transcriptional imbalance in the kdm A deletion mutant may contribute to the lethal phenotype observed upon exposure of mutant cells to low‐density visible light on solid medium. Although KdmA acts as transcriptional co‐repressor of primary metabolism genes, it is required for full expression of several genes involved in biosynthesis of secondary metabolites. John Wiley and Sons Inc. 2015-04-11 2015-05 /pmc/articles/PMC4949671/ /pubmed/25712266 http://dx.doi.org/10.1111/mmi.12977 Text en © 2015 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Gacek‐Matthews, Agnieszka Noble, Luke M. Gruber, Clemens Berger, Harald Sulyok, Michael Marcos, Ana T. Strauss, Joseph Andrianopoulos, Alex KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A spergillus nidulans |
title |
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A
spergillus nidulans
|
title_full |
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A
spergillus nidulans
|
title_fullStr |
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A
spergillus nidulans
|
title_full_unstemmed |
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A
spergillus nidulans
|
title_short |
KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in A
spergillus nidulans
|
title_sort | kdma, a histone h3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in a
spergillus nidulans |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949671/ https://www.ncbi.nlm.nih.gov/pubmed/25712266 http://dx.doi.org/10.1111/mmi.12977 |
work_keys_str_mv | AT gacekmatthewsagnieszka kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT noblelukem kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT gruberclemens kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT bergerharald kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT sulyokmichael kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT marcosanat kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT straussjoseph kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans AT andrianopoulosalex kdmaahistoneh3demethylasewithbipartitefunctiondifferentiallyregulatesprimaryandsecondarymetabolisminaspergillusnidulans |