The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response. Issue 15 (2nd August 2021)
- Record Type:
- Journal Article
- Title:
- The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response. Issue 15 (2nd August 2021)
- Main Title:
- The C-terminal region of yeast ubiquitin–protein ligase Not4 mediates its cellular localization and stress response
- Authors:
- Palermo, Vanessa
Stirpe, Mariarita
Bianchi, Michele Maria
Rinaldi, Teresa
Cirigliano, Angela
Ragnini-Wilson, Antonella
Falcone, Claudio
Mazzoni, Cristina - Abstract:
- ABSTRACT: Transient modification of the environment involves the expression of specific genes and degradation of mRNAs and proteins. How these events are linked is poorly understood. CCR4-NOT is an evolutionary conserved complex involved in transcription initiation and mRNA degradation. In this paper, we report that the yeast Not4 localizes in cytoplasmic foci after cellular stress. We focused our attention on the functional characterization of the C-terminus of the Not4 protein. Molecular dissection of this region indicates that the removal of the last 120 amino acids, does not affect protein localization and function, in that the protein is still able to suppress the thermosensitivity observed in the not4Δ mutant. In addition, such shortened form of Not4, as well its absence, increases the transcription of stress-responsive genes conferring to the cell high resistance to the oxidative stress. On the contrary, the last C-terminal 211 amino acids are required for proper Not4 localization at cytoplasmic foci after stress. This truncated version of Not4 fails to increase the transcription of the stress genes, is more stable and seems to be toxic to cells undergoing oxidative stress. Abstract : The C-terminal region of Not4 ubiquitin ligase mediates the formation of cytoplasmic foci after stress. In addition, this region contains positive and negative elements that influence cell resistance to hydrogen peroxide.
- Is Part Of:
- FEMS microbiology letters. Volume 368:Issue 15(2021)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 368:Issue 15(2021)
- Issue Display:
- Volume 368, Issue 15 (2021)
- Year:
- 2021
- Volume:
- 368
- Issue:
- 15
- Issue Sort Value:
- 2021-0368-0015-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-08-02
- Subjects:
- yeast -- stress response -- E3 ubiquitin ligase -- gene expression -- protein aggregation
Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/femsle/fnab097 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
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- 25619.xml