8f9y | pdb_00008f9y
SAL1 from Arabidopsis thaliana
Structural highlights
FunctionDPNP1_ARATH Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing.[1] [2] [3] Publication Abstract from PubMedIntracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3'-phosphoadenosine 5'-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom. Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase.,Chan KX, Mabbitt PD, Phua SY, Mueller JW, Nisar N, Gigolashvili T, Stroeher E, Grassl J, Arlt W, Estavillo GM, Jackson CJ, Pogson BJ Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):E4567-E4576. Epub 2016 Jul 18. PMID:27432987[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
