PMID- 18852264 OWN - NLM STAT- MEDLINE DCOM- 20090204 LR - 20240109 IS - 0021-9258 (Print) IS - 1083-351X (Electronic) IS - 0021-9258 (Linking) VI - 283 IP - 49 DP - 2008 Dec 5 TI - Ascorbate peroxidase 1 plays a key role in the response of Arabidopsis thaliana to stress combination. PG - 34197-203 LID - 10.1074/jbc.M806337200 [doi] AB - Within their natural habitat plants are subjected to a combination of different abiotic stresses, each with the potential to exacerbate the damage caused by the others. One of the most devastating stress combinations for crop productivity, which frequently occurs in the field, is drought and heat stress. In this study we conducted proteomic and metabolic analysis of Arabidopsis thaliana plants subjected to a combination of drought and heat stress. We identified 45 different proteins that specifically accumulated in Arabidopsis in response to the stress combination. These included enzymes involved in reactive oxygen detoxification, malate metabolism, and the Calvin cycle. The accumulation of malic enzyme during the combined stress corresponded with enhanced malic enzyme activity, a decrease in malic acid, and lower amounts of oxaloacetate, suggesting that malate metabolism plays an important role in the response of Arabidopsis to the stress combination. Cytosolic ascorbate peroxidase 1 (APX1) protein and mRNA accumulated during the stress combination. When exposed to heat stress combined with drought, an APX1-deficient mutant (apx1) accumulated more hydrogen peroxide and was significantly more sensitive to the stress combination than wild type. In contrast, mutants deficient in thylakoid or stromal/mitochondrial APXs were not more sensitive to the stress combination than apx1 or wild type. Our findings suggest that cytosolic APX1 plays a key role in the acclimation of plants to a combination of drought and heat stress. FAU - Koussevitzky, Shai AU - Koussevitzky S AD - Department of Biochemistry and Molecular Biology, University of Nevada, Reno, Nevada 89557, USA. FAU - Suzuki, Nobuhiro AU - Suzuki N FAU - Huntington, Serena AU - Huntington S FAU - Armijo, Leigh AU - Armijo L FAU - Sha, Wei AU - Sha W FAU - Cortes, Diego AU - Cortes D FAU - Shulaev, Vladimir AU - Shulaev V FAU - Mittler, Ron AU - Mittler R LA - eng GR - P20 RR16464-05/RR/NCRR NIH HHS/United States GR - RR-03-008/RR/NCRR NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, Non-P.H.S. DEP - 20081013 PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Arabidopsis Proteins) RN - 0 (Chloroplast Proteins) RN - 0 (RNA, Messenger) RN - 059QF0KO0R (Water) RN - BBX060AN9V (Hydrogen Peroxide) RN - EC 1.11.1.- (Peroxidases) RN - EC 1.11.1.11 (APXS protein, Arabidopsis) RN - EC 1.11.1.11 (Ascorbate Peroxidases) SB - IM MH - Arabidopsis/*enzymology MH - Arabidopsis Proteins MH - Ascorbate Peroxidases MH - Chloroplast Proteins MH - Chromatography, Liquid MH - Cytosol/enzymology/metabolism MH - Droughts MH - Gene Expression Regulation, Plant MH - Hot Temperature MH - Hydrogen Peroxide/chemistry MH - Mass Spectrometry MH - Models, Biological MH - Mutation MH - Peroxidases/*genetics/*physiology MH - Proteomics/methods MH - RNA, Messenger/metabolism MH - Time Factors MH - Water/chemistry PMC - PMC2590703 EDAT- 2008/10/15 09:00 MHDA- 2009/02/05 09:00 PMCR- 2009/12/05 CRDT- 2008/10/15 09:00 PHST- 2008/10/15 09:00 [pubmed] PHST- 2009/02/05 09:00 [medline] PHST- 2008/10/15 09:00 [entrez] PHST- 2009/12/05 00:00 [pmc-release] AID - S0021-9258(20)65277-2 [pii] AID - 34197 [pii] AID - 10.1074/jbc.M806337200 [doi] PST - ppublish SO - J Biol Chem. 2008 Dec 5;283(49):34197-203. doi: 10.1074/jbc.M806337200. Epub 2008 Oct 13.