| Plastidic phosphatidic acid phosphatases identified in a distinct subfamily of lipid phosphate phosphatases with prokaryotic origin. | |
| | |
MedLine Citation:
|
PMID: 17652095 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Plastidic phosphatidic acid phosphatase (PAP) dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes. Despite its functional importance, the molecular characteristics and phylogenetic origin of plastidic PAP were unknown because no potential homologs have been found. Here, we report the isolation and characterization of plastidic PAPs in Arabidopsis that belong to a distinct lipid phosphate phosphatase (LPP) subfamily with prokaryotic origin. Because no homolog of mammalian LPP was found in cyanobacteria, we sought an LPP ortholog in a more primitive organism, Chlorobium tepidum, and its homologs in cyanobacteria. Arabidopsis had five homologs of cyanobacterial LPP, three of which (LPP gamma, LPP epsilon 1, and LPP epsilon 2) localized to chloroplasts. Complementation of yeast Delta dpp1 Delta lpp1 Delta pah1 by plastidic LPPs rescued the relevant phenotype in vitro and in vivo, suggesting that they function as PAPs. Of the three LPPs, LPP gamma activity best resembled the native activity. The three plastidic LPPs were differentially expressed both in green and nongreen tissues, with LPP gamma expressed the highest in shoots. A knock-out mutant for LPP gamma could not be obtained, although a lpp epsilon 1 lpp epsilon 2 double knock-out showed no significant changes in lipid composition. However, lpp gamma homozygous mutant was isolated only under ectopic overexpression of LPP gamma, suggesting that loss of LPP gamma may cause lethal effect on plant viability. Thus, in Arabidopsis, there are three isoforms of plastidic PAP that belong to a distinct subfamily of LPP, and LPP gamma may be the primary plastidic PAP. |
| | |
Authors:
|
Yuki Nakamura; Mami Tsuchiya; Hiroyuki Ohta |
Related Documents
:
|
3625705 - Gamma-aminobutyric acid esters. 3. synthesis, brain uptake, and pharmacological propert... 3761305 - Inactivation of gamma-aminobutyric acid aminotransferase by (s,e)-4-amino-5-fluoropent-... 8516315 - Localized 1h nmr measurements of gamma-aminobutyric acid in human brain in vivo. 3552825 - Ultrastructural localization of gamma amino butyric acid immunoreactivity in b cells of... 10792535 - Dose-response relationships. a model for describing interactions, and its application t... 6260195 - The kinetic mechanism of inhibition of liver pyridoxal kinase with tryptophan metabolites. |
Publication Detail:
|
Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2007-07-24 |
Journal Detail:
|
Title: The Journal of biological chemistry Volume: 282 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2007 Sep |
Date Detail:
|
Created Date: 2007-09-24 Completed Date: 2007-11-08 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
|
Languages: eng Pagination: 29013-21 Citation Subset: IM |
Affiliation:
|
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B-65 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Arabidopsis
/
enzymology,
genetics* Arabidopsis Proteins / biosynthesis, genetics* Chlorobium / enzymology, genetics* Chloroplasts / enzymology, genetics* Evolution, Molecular* Gene Expression Regulation, Enzymologic / physiology* Gene Expression Regulation, Plant / physiology* Genetic Complementation Test Isoenzymes / biosynthesis, genetics Mutation Phosphatidate Phosphatase / biosynthesis, genetics* Phylogeny Plants, Genetically Modified / enzymology, genetics Saccharomyces cerevisiae / enzymology, genetics Sequence Homology, Amino Acid |
| Chemical | |
Reg. No./Substance:
|
0/Arabidopsis Proteins; 0/Isoenzymes; EC 3.1.3.-/lipid phosphate phosphatase; EC 3.1.3.4/Phosphatidate Phosphatase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Sac...
Next Document: Global assessment of combinatorial post-translational modification of core histones in yeast using c...