LPA66 Is Required for Editing psbF Chloroplast Transcripts in Arabidopsis

To gain insight into the molecular mechanism of RNA editing, we have characterized the low psii accumulation66 (lpa66) Arabidopsis (Arabidopsis thaliana) mutant, which displays a high chlorophyll fluorescence phenotype. Its perturbed chlorophyll fluorescence is reflected in reduced levels of photosy...

Full description

Saved in:
Bibliographic Details
Published in:Plant physiology (Bethesda) 2009-07, Vol.150 (3), p.1260-1271
Main Authors: Cai, Wenhe, Ji, Daili, Peng, Lianwei, Guo, Jinkui, Ma, Jinfang, Zou, Meijuan, Lu, Congming, Zhang, Lixin
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - genetics
Arabidopsis Proteins - physiology
Bioenergetics and Photosynthesis
Biological and medical sciences
Chlorophylls
Chloroplasts
Chloroplasts - metabolism
Cloning, Molecular
Fluorescence
Fundamental and applied biological sciences. Psychology
Molecular Sequence Data
Mutation
Photosystem II Protein Complex - metabolism
Plant cells
Plant physiology and development
Plants
Plastids
Protein Biosynthesis - genetics
Protein Structure, Tertiary
Proteins
RNA
RNA editing
RNA Editing - genetics
RNA Editing - physiology
RNA, Messenger - metabolism
Sequence Alignment
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:To gain insight into the molecular mechanism of RNA editing, we have characterized the low psii accumulation66 (lpa66) Arabidopsis (Arabidopsis thaliana) mutant, which displays a high chlorophyll fluorescence phenotype. Its perturbed chlorophyll fluorescence is reflected in reduced levels of photosystem II (PSII) proteins. In vivo protein labeling showed that synthesis rates of the PSII reaction center protein D1/D2 were lower, and turnover rates of PSII core proteins higher, than in wild-type counterparts. The assembly of newly synthesized proteins into PSII occurs in the lpa66 mutant but with reduced efficiency compared with the wild type. LPA66 encodes a chloroplast protein of the pentatricopeptide repeat family. In lpa66 mutants, editing of psbF that converts serine to phenylalanine is specifically impaired. Thus, LPA66 is specifically required for editing the psbF transcripts in Arabidopsis, and the amino acid alternation due to lack of editing strongly affects the efficiency of the assembly of PSII complexes.
ISSN:0032-0889
1532-2548
1532-2548
DOI:10.1104/pp.109.136812