Extrachloroplastic PP7L Functions in Chloroplast Development and Abiotic Stress Tolerance. Issue 1 (13th February 2019)
- Record Type:
- Journal Article
- Title:
- Extrachloroplastic PP7L Functions in Chloroplast Development and Abiotic Stress Tolerance. Issue 1 (13th February 2019)
- Main Title:
- Extrachloroplastic PP7L Functions in Chloroplast Development and Abiotic Stress Tolerance
- Authors:
- Xu, Duorong
Marino, Giada
Klingl, Andreas
Enderle, Beatrix
Monte, Elena
Kurth, Joachim
Hiltbrunner, Andreas
Leister, Dario
Kleine, Tatjana - Abstract:
- Abstract : Arabidopsis protein phosphatase PP7-like (PP7L) is a predominantly nuclear-localized protein that promotes chloroplast translation and development, thus contributing to abiotic stress tolerance. Abstract: Chloroplast biogenesis is indispensable for proper plant development and environmental acclimation. In a screen for mutants affected in photosynthesis, we identified the protein phosphatase7 - like ( pp7l ) mutant, which displayed delayed chloroplast development in cotyledons and young leaves. PP7L, PP7, and PP7-long constitute a subfamily of phosphoprotein phosphatases. PP7 is thought to transduce a blue-light signal perceived by crys and phy a that induces expression of SIGMA FACTOR5 (SIG5). We observed that, like PP7, PP7L was predominantly localized to the nucleus in Arabidopsis ( Arabidopsis thaliana ), and the pp7l phenotype was similar to that of the sig6 mutant. However, SIG6 expression was unaltered in pp7l mutants. Instead, loss of PP7L compromised translation and ribosomal RNA (rRNA) maturation in chloroplasts, pointing to a distinct mechanism influencing chloroplast development. Promoters of genes deregulated in pp7l - 1 were enriched in PHYTOCHROME-INTERACTING FACTOR (PIF)-binding motifs and the transcriptome of pp7l - 1 resembled those of pif and CONSTITUTIVE PHOTOMORPHOGENESIS1 (COP1) signalosome complex ( csn ) mutants. However, pif and csn mutants, as well as cop1, cryptochromes (cry)1 cry2, and phytochromes (phy)A phyB mutants, do not share theAbstract : Arabidopsis protein phosphatase PP7-like (PP7L) is a predominantly nuclear-localized protein that promotes chloroplast translation and development, thus contributing to abiotic stress tolerance. Abstract: Chloroplast biogenesis is indispensable for proper plant development and environmental acclimation. In a screen for mutants affected in photosynthesis, we identified the protein phosphatase7 - like ( pp7l ) mutant, which displayed delayed chloroplast development in cotyledons and young leaves. PP7L, PP7, and PP7-long constitute a subfamily of phosphoprotein phosphatases. PP7 is thought to transduce a blue-light signal perceived by crys and phy a that induces expression of SIGMA FACTOR5 (SIG5). We observed that, like PP7, PP7L was predominantly localized to the nucleus in Arabidopsis ( Arabidopsis thaliana ), and the pp7l phenotype was similar to that of the sig6 mutant. However, SIG6 expression was unaltered in pp7l mutants. Instead, loss of PP7L compromised translation and ribosomal RNA (rRNA) maturation in chloroplasts, pointing to a distinct mechanism influencing chloroplast development. Promoters of genes deregulated in pp7l - 1 were enriched in PHYTOCHROME-INTERACTING FACTOR (PIF)-binding motifs and the transcriptome of pp7l - 1 resembled those of pif and CONSTITUTIVE PHOTOMORPHOGENESIS1 (COP1) signalosome complex ( csn ) mutants. However, pif and csn mutants, as well as cop1, cryptochromes (cry)1 cry2, and phytochromes (phy)A phyB mutants, do not share the pp7l photosynthesis phenotype. PhyB protein levels were elevated in pp7l mutants, but phyB overexpression plants did not resemble pp7l . These results indicate that PP7L operates through a different pathway and that the control of greening and photosystem biogenesis can be separated. The lack of PP7L increased susceptibility to salt and high-light stress, whereas PP7L overexpression conferred resistance to high-light stress. Strikingly, PP7L was specifically recruited to Brassicales for the regulation of chloroplast development. This study adds another player involved in chloroplast biogenesis. … (more)
- Is Part Of:
- Plant physiology. Volume 180:Issue 1(2019)
- Journal:
- Plant physiology
- Issue:
- Volume 180:Issue 1(2019)
- Issue Display:
- Volume 180, Issue 1 (2019)
- Year:
- 2019
- Volume:
- 180
- Issue:
- 1
- Issue Sort Value:
- 2019-0180-0001-0000
- Page Start:
- 323
- Page End:
- 341
- Publication Date:
- 2019-02-13
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.19.00070 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22246.xml