The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans.
A mutation screen in Aspergillus nidulans uncovered mutations in the acdX gene that led to altered repression by acetate, but not by glucose. AcdX of A. nidulans is highly conserved with Spt8p of Saccharomyces cerevisiae, and since Spt8p is a component of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) co...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
|
| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3676421?pdf=render |
| _version_ | 1819012924677554176 |
|---|---|
| author | Paraskevi Georgakopoulos Robin A Lockington Joan M Kelly |
| author_facet | Paraskevi Georgakopoulos Robin A Lockington Joan M Kelly |
| author_sort | Paraskevi Georgakopoulos |
| collection | DOAJ |
| description | A mutation screen in Aspergillus nidulans uncovered mutations in the acdX gene that led to altered repression by acetate, but not by glucose. AcdX of A. nidulans is highly conserved with Spt8p of Saccharomyces cerevisiae, and since Spt8p is a component of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex, the SAGA complex may have a role in acetate repression in A. nidulans. We used a bioinformatic approach to identify genes encoding most members of the SAGA complex in A. nidulans, and a proteomic analysis to confirm that most protein components identified indeed exist as a complex in A. nidulans. No apparent compositional differences were detected in mycelia cultured in acetate compared to glucose medium. The methods used revealed apparent differences between Yeast and A. nidulans in the deubiquitination (DUB) module of the complex, which in S. cerevisiae consists of Sgf11p, Sus1p, and Ubp8p. Although a convincing homologue of S. cerevisiae Ubp8p was identified in the A. nidulans genome, there were no apparent homologues for Sus1p and Sgf11p. In addition, when the SAGA complex was purified from A. nidulans, members of the DUB module were not co-purified with the complex, indicating that functional homologues of Sus1p and Sgf11p were not part of the complex. Thus, deubiquitination of H2B-Ub in stress conditions is likely to be regulated differently in A. nidulans compared to S. cerevisiae. |
| first_indexed | 2024-12-21T01:51:47Z |
| format | Article |
| id | doaj.art-1a8d8f7843e844e2b0a7046c08b60e77 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T01:51:47Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-1a8d8f7843e844e2b0a7046c08b60e772022-12-21T19:19:52ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0186e6522110.1371/journal.pone.0065221The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans.Paraskevi GeorgakopoulosRobin A LockingtonJoan M KellyA mutation screen in Aspergillus nidulans uncovered mutations in the acdX gene that led to altered repression by acetate, but not by glucose. AcdX of A. nidulans is highly conserved with Spt8p of Saccharomyces cerevisiae, and since Spt8p is a component of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex, the SAGA complex may have a role in acetate repression in A. nidulans. We used a bioinformatic approach to identify genes encoding most members of the SAGA complex in A. nidulans, and a proteomic analysis to confirm that most protein components identified indeed exist as a complex in A. nidulans. No apparent compositional differences were detected in mycelia cultured in acetate compared to glucose medium. The methods used revealed apparent differences between Yeast and A. nidulans in the deubiquitination (DUB) module of the complex, which in S. cerevisiae consists of Sgf11p, Sus1p, and Ubp8p. Although a convincing homologue of S. cerevisiae Ubp8p was identified in the A. nidulans genome, there were no apparent homologues for Sus1p and Sgf11p. In addition, when the SAGA complex was purified from A. nidulans, members of the DUB module were not co-purified with the complex, indicating that functional homologues of Sus1p and Sgf11p were not part of the complex. Thus, deubiquitination of H2B-Ub in stress conditions is likely to be regulated differently in A. nidulans compared to S. cerevisiae.http://europepmc.org/articles/PMC3676421?pdf=render |
| spellingShingle | Paraskevi Georgakopoulos Robin A Lockington Joan M Kelly The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. PLoS ONE |
| title | The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. |
| title_full | The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. |
| title_fullStr | The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. |
| title_full_unstemmed | The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. |
| title_short | The Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex in Aspergillus nidulans. |
| title_sort | spt ada gcn5 acetyltransferase saga complex in aspergillus nidulans |
| url | http://europepmc.org/articles/PMC3676421?pdf=render |
| work_keys_str_mv | AT paraskevigeorgakopoulos thesptadagcn5acetyltransferasesagacomplexinaspergillusnidulans AT robinalockington thesptadagcn5acetyltransferasesagacomplexinaspergillusnidulans AT joanmkelly thesptadagcn5acetyltransferasesagacomplexinaspergillusnidulans AT paraskevigeorgakopoulos sptadagcn5acetyltransferasesagacomplexinaspergillusnidulans AT robinalockington sptadagcn5acetyltransferasesagacomplexinaspergillusnidulans AT joanmkelly sptadagcn5acetyltransferasesagacomplexinaspergillusnidulans |