English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Abnormal Physiological and Molecular Mutant Phenotypes Link Chloroplast Polynucleotide Phosphorylase to the Phosphorus Deprivation Response in Arabidopsis

Marchive, C., Yehudai-Resheff, S., Germain, A., Fei, Z. J., Jiang, X. S., Judkins, J., et al. (2009). Abnormal Physiological and Molecular Mutant Phenotypes Link Chloroplast Polynucleotide Phosphorylase to the Phosphorus Deprivation Response in Arabidopsis. Plant Physiology, 151(2), 905-924. doi:10.1104/pp.109.145144.

Item is

Files

show Files
hide Files
:
Marchive-2009-Abnormal Physiologic.pdf (Any fulltext), 4MB
Name:
Marchive-2009-Abnormal Physiologic.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Marchive, C.1, Author
Yehudai-Resheff, S.1, Author
Germain, A.1, Author
Fei, Z. J.1, Author
Jiang, X. S.1, Author
Judkins, J.1, Author
Wu, H.1, Author
Fernie, A. R.2, Author           
Fait, A.2, Author           
Stern, D. B.1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Central Metabolism, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753339              

Content

show
hide
Free keywords: programmed cell-death methylerythritol phosphate-pathway rna-binding proteins transcription factor er-body starvation responses poly(a) polymerase root architecture acid biosynthesis escherichia-coli
 Abstract: A prominent enzyme in organellar RNA metabolism is the exoribonuclease polynucleotide phosphorylase (PNPase), whose reversible activity is governed by the nucleotide diphosphate-inorganic phosphate ratio. In Chlamydomonas reinhardtii, PNPase regulates chloroplast transcript accumulation in response to phosphorus (P) starvation, and PNPase expression is repressed by the response regulator PSR1 (for PHOSPHORUS STARVATION RESPONSE1) under these conditions. Here, we investigated the role of PNPase in the Arabidopsis (Arabidopsis thaliana) P deprivation response by comparing wild-type and pnp mutant plants with respect to their morphology, metabolite profiles, and transcriptomes. We found that P-deprived pnp mutants develop aborted clusters of lateral roots, which are characterized by decreased auxin responsiveness and cell division, and exhibit cell death at the root tips. Electron microscopy revealed that the collapse of root organelles is enhanced in the pnp mutant under P deprivation and occurred with low frequency under P-replete conditions. Global analyses of metabolites and transcripts were carried out to understand the molecular bases of these altered P deprivation responses. We found that the pnp mutant expresses some elements of the deprivation response even when grown on a full nutrient medium, including altered transcript accumulation, although its total and inorganic P contents are not reduced. The pnp mutation also confers P status-independent responses, including but not limited to stress responses. Taken together, our data support the hypothesis that the activity of the chloroplast PNPase is involved in plant acclimation to P availability and that it may help maintain an appropriate balance of P metabolites even under normal growth conditions.

Details

show
hide
Language(s): eng - English
 Dates: 2009-08-282009
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: ISI:000270389500034
DOI: 10.1104/pp.109.145144
ISSN: 0032-0889 (Print)0032-0889 (Linking)
URI: ://000270389500034http://www.jstor.org/stable/pdfplus/40537821.pdf
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Plant Physiology
  Other : Plant Physiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Bethesda, Md. : American Society of Plant Biologists
Pages: - Volume / Issue: 151 (2) Sequence Number: - Start / End Page: 905 - 924 Identifier: ISSN: 0032-0889
CoNE: https://pure.mpg.de/cone/journals/resource/991042744294438