Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation. (16th September 2020)
- Record Type:
- Journal Article
- Title:
- Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation. (16th September 2020)
- Main Title:
- Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation
- Authors:
- Li, Mingai
Barbaro, Enrico
Bellini, Erika
Saba, Alessandro
Sanità di Toppi, Luigi
Varotto, Claudio - Editors:
- Cuypers, Ann
- Abstract:
- Abstract : The characterization of Marchantia polymorpha phytochelatin synthase provides novel insights into the evolutionary function of the enzyme's elusive C-terminus as a regulatory domain inhibiting enzyme overactivation by metal ions. Abstract: Phytochelatin synthases (PCSs) play essential roles in detoxification of a broad range of heavy metals in plants and other organisms. Until now, however, no PCS gene from liverworts, the earliest branch of land plants and possibly the first one to acquire a PCS with a C-terminal domain, has been characterized. In this study, we isolated and functionally characterized the first PCS gene from a liverwort, Marchantia polymorpha ( MpPCS ). MpPCS is constitutively expressed in all organs examined, with stronger expression in thallus midrib. The gene expression is repressed by Cd 2+ and Zn 2+ . The ability of MpPCS to increase heavy metal resistance in yeast and to complement cad1-3 (the null mutant of the Arabidopsis ortholog AtPCS1 ) proves its function as the only PCS from M. polymorpha . Site-directed mutagenesis of the most conserved cysteines of the C-terminus of the enzyme further uncovered that two twin-cysteine motifs repress, to different extents, enzyme activation by heavy metal exposure. These results highlight an ancestral function of the PCS elusive C-terminus as a regulatory domain inhibiting enzyme overactivation by essential and non-essential heavy metals. The latter finding may be relevant for obtaining crops withAbstract : The characterization of Marchantia polymorpha phytochelatin synthase provides novel insights into the evolutionary function of the enzyme's elusive C-terminus as a regulatory domain inhibiting enzyme overactivation by metal ions. Abstract: Phytochelatin synthases (PCSs) play essential roles in detoxification of a broad range of heavy metals in plants and other organisms. Until now, however, no PCS gene from liverworts, the earliest branch of land plants and possibly the first one to acquire a PCS with a C-terminal domain, has been characterized. In this study, we isolated and functionally characterized the first PCS gene from a liverwort, Marchantia polymorpha ( MpPCS ). MpPCS is constitutively expressed in all organs examined, with stronger expression in thallus midrib. The gene expression is repressed by Cd 2+ and Zn 2+ . The ability of MpPCS to increase heavy metal resistance in yeast and to complement cad1-3 (the null mutant of the Arabidopsis ortholog AtPCS1 ) proves its function as the only PCS from M. polymorpha . Site-directed mutagenesis of the most conserved cysteines of the C-terminus of the enzyme further uncovered that two twin-cysteine motifs repress, to different extents, enzyme activation by heavy metal exposure. These results highlight an ancestral function of the PCS elusive C-terminus as a regulatory domain inhibiting enzyme overactivation by essential and non-essential heavy metals. The latter finding may be relevant for obtaining crops with decreased root to shoot mobility of cadmium, thus preventing its accumulation in the food chain. … (more)
- Is Part Of:
- Journal of experimental botany. Volume 71:Number 20(2020)
- Journal:
- Journal of experimental botany
- Issue:
- Volume 71:Number 20(2020)
- Issue Display:
- Volume 71, Issue 20 (2020)
- Year:
- 2020
- Volume:
- 71
- Issue:
- 20
- Issue Sort Value:
- 2020-0071-0020-0000
- Page Start:
- 6655
- Page End:
- 6669
- Publication Date:
- 2020-09-16
- Subjects:
- Cadmium -- C-terminal domain -- Marchantia polymorpha -- overactivation -- phytochelatin -- phytochelatin synthase -- site-directed mutagenesis -- twin-cysteine motif -- zinc
Botany -- Periodicals
Botany, Experimental -- Periodicals
Plant physiology -- Periodicals
580 - Journal URLs:
- http://ukcatalogue.oup.com/ ↗
http://jxb.oxfordjournals.org/ ↗ - DOI:
- 10.1093/jxb/eraa386 ↗
- Languages:
- English
- ISSNs:
- 0022-0957
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4981.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 15592.xml