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Roles of Arabidopsis patatin-related phospholipases a in root development are related to auxin responses and phosphate deficiency.

Authors :
Rietz S
Dermendjiev G
Oppermann E
Tafesse FG
Effendi Y
Holk A
Parker JE
Teige M
Scherer GF
Source :
Molecular plant [Mol Plant] 2010 May; Vol. 3 (3), pp. 524-38. Date of Electronic Publication: 2010 Jan 06.
Publication Year :
2010

Abstract

Phospholipase A enzymes cleave phospho- and galactolipids to generate free fatty acids and lysolipids that function in animal and plant hormone signaling. Here, we describe three Arabidopsis patatin-related phospholipase A (pPLA) genes AtPLAIVA, AtPLAIVB, and AtPLAIVC and their corresponding proteins. Loss-of-function mutants reveal roles for these pPLAs in roots during normal development and under phosphate deprivation. AtPLAIVA is expressed strongly and exclusively in roots and AtplaIVA-null mutants have reduced lateral root development, characteristic of an impaired auxin response. By contrast, AtPLAIVB is expressed weakly in roots, cotyledons, and leaves but is transcriptionally induced by auxin, although AtplaIVB mutants develop normally. AtPLAIVC is expressed in the floral gynaecium and is induced by abscisic acid (ABA) or phosphate deficiency in roots. While an AtplaIVC-1 loss-of-function mutant displays ABA responsiveness, it exhibits an impaired response to phosphate deficiency during root development. Recombinant AtPLA proteins hydrolyze preferentially galactolipids and, less efficiently, phospholipids, although these enzymes are not localized in chloroplasts. We find that AtPLAIVA and AtPLAIVB are phosphorylated by calcium-dependent protein kinases in vitro and this enhances their activities on phosphatidylcholine but not on phosphatidylglycerol. Taken together, the data reveal novel functions of pPLAs in root development with individual roles at the interface between phosphate deficiency and auxin signaling.

Details

Language :
English
ISSN :
1674-2052
Volume :
3
Issue :
3
Database :
MEDLINE
Journal :
Molecular plant
Publication Type :
Academic Journal
Accession number :
20053799
Full Text :
https://doi.org/10.1093/mp/ssp109