See the published version of this preprint at Epigenetics & Chromatin.
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Research
Susana Rodriguez-Navarro
Consejo Superior de Investigaciones Cientificas
Corresponding Author
ORCiD: https://orcid.org/0000-0001-7472-3111
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Background: Histone H2B deubiquitination is performed by numerous deubiquitinases in eukaryotic cells including Ubp8, the catalytic subunit of the tetrameric deubiquitination module (DUBm: Ubp8; Sus1; Sgf11; Sgf73) of the Spt-Ada-Gcn5 acetyltransferase (SAGA). Ubp8 is linked to the rest of SAGA through Sgf73 and is activated by the adaptors Sus1 and Sgf11. It is unknown if DUBm/Ubp8 might also work in a SAGA-independent manner.
Results: Here we report that a tetrameric DUBm is assembled independently of the SAGA-CORE components SPT7, ADA1 and SPT20. In the absence of SPT7, i.e. independent of the SAGA complex, Ubp8 and Sus1 are poorly recruited to SAGA-dependent genes and to chromatin. Notably, cells lacking Spt7 or Ada1, but not Spt20, show lower levels of nuclear Ubp8 than wild type cells, suggesting a possible role for SAGA-CORE subunits in Ubp8 localization. Last, deletion of SPT7 leads to defects in Ubp8 deubiquitinase activity in in vivo and in vitroassays.
Conclusions: Collectively, our studies show that the DUBm tetrameric structure can form without a complete intact SAGA-CORE complex and that it includes full length Sgf73. However, subunits of this SAGA-CORE influence DUBm association with chromatin, its localization and its activity.
Keywords
SAGA, histone deubiquitination, Spt7, transcription, yeast
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CURRENT STATUS: Published
View the published article at Epigenetics & Chromatin.
Version 2
Posted 22 Sep, 2020
No community comments so far
Editorial decision: Accept
On 09 Oct, 2020
Reviewers invited
Invitations sent on 23 Sep, 2020
Editor assigned
On 20 Sep, 2020
Submission checks complete
On 19 Sep, 2020
Editor invited
On 19 Sep, 2020
No comments provided
Editorial decision: Major revision
On 22 Aug, 2020
Review #2 received
Received 13 Aug, 2020
Reviewer #2 agreed
On 30 Jul, 2020
Review #1 received
Received 19 Jul, 2020
Reviewers invited
Invitations sent on 09 Jul, 2020
Reviewer #1 agreed
On 09 Jul, 2020
Editor assigned
On 23 Jun, 2020
Editor invited
On 22 Jun, 2020
Submission checks complete
On 31 May, 2020
First submitted
On 30 May, 2020
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See the published version of this preprint at Epigenetics & Chromatin.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research
Susana Rodriguez-Navarro
Consejo Superior de Investigaciones Cientificas
Corresponding Author
ORCiD: https://orcid.org/0000-0001-7472-3111
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at Epigenetics & Chromatin.
Version 2
Posted 22 Sep, 2020
No community comments so far
Editorial decision: Accept
On 09 Oct, 2020
Reviewers invited
Invitations sent on 23 Sep, 2020
Editor assigned
On 20 Sep, 2020
Submission checks complete
On 19 Sep, 2020
Editor invited
On 19 Sep, 2020
No comments provided
Editorial decision: Major revision
On 22 Aug, 2020
Review #2 received
Received 13 Aug, 2020
Reviewer #2 agreed
On 30 Jul, 2020
Review #1 received
Received 19 Jul, 2020
Reviewers invited
Invitations sent on 09 Jul, 2020
Reviewer #1 agreed
On 09 Jul, 2020
Editor assigned
On 23 Jun, 2020
Editor invited
On 22 Jun, 2020
Submission checks complete
On 31 May, 2020
First submitted
On 30 May, 2020
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at Epigenetics & Chromatin.
Background: Histone H2B deubiquitination is performed by numerous deubiquitinases in eukaryotic cells including Ubp8, the catalytic subunit of the tetrameric deubiquitination module (DUBm: Ubp8; Sus1; Sgf11; Sgf73) of the Spt-Ada-Gcn5 acetyltransferase (SAGA). Ubp8 is linked to the rest of SAGA through Sgf73 and is activated by the adaptors Sus1 and Sgf11. It is unknown if DUBm/Ubp8 might also work in a SAGA-independent manner.
Results: Here we report that a tetrameric DUBm is assembled independently of the SAGA-CORE components SPT7, ADA1 and SPT20. In the absence of SPT7, i.e. independent of the SAGA complex, Ubp8 and Sus1 are poorly recruited to SAGA-dependent genes and to chromatin. Notably, cells lacking Spt7 or Ada1, but not Spt20, show lower levels of nuclear Ubp8 than wild type cells, suggesting a possible role for SAGA-CORE subunits in Ubp8 localization. Last, deletion of SPT7 leads to defects in Ubp8 deubiquitinase activity in in vivo and in vitroassays.
Conclusions: Collectively, our studies show that the DUBm tetrameric structure can form without a complete intact SAGA-CORE complex and that it includes full length Sgf73. However, subunits of this SAGA-CORE influence DUBm association with chromatin, its localization and its activity.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
This is a list of supplementary files associated with this preprint. Click to download.
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