title: The function of LPR1 is controlled by an element in the promoter and is independent of SUMO E3 Ligase SIZ1 in response to low Pi stress in Arabidopsis thaliana.
abstract: In Arabidopsis thaliana, there exist many typical responses to low phosphate (LP) stress, such as inhibition of primary root elongation, proliferation of lateral roots and accumulation of anthocyanin in leaves. The physiological, genetic and molecular mechanisms of these developmental responses remain undefined. We have isolated a phosphorus starvation-insensitive (psi) mutant. The mutant shows impaired inhibition of primary root growth, reduction of root hair growth and reduction of anthocyanin accumulation compared with the wild-type (WT) plants under an LP level. CycB1;1::GUS (cyclin B1;1::beta-glucuronidase) staining suggests that the mutant has a higher ability to maintain cell elongation and cell division than the WT. The genetic analysis and gene cloning indicate that psi is a new allele of lpr1 and that an AC-repeat element in the promoter plays important roles in controlling the expression of LPR1. The psi mutant also shows less sensitivity to auxin treatment compared with the WT and the mutant has an enhanced higher ability to maintain the auxin response in the root tip under LP. However, enhancing the auxin response in the quiescent center cannot mimic the mutant phenotype. These observations suggest that LPR1 is involved in the regulation of the auxin response to Pi starvation and auxin is probably not the only factor affected for maintaining the long-root phenotype under LP stress. Our results also indicate that the function of LPR1 is probably independent of SUMO E3 ligase SIZ1 in response to Pi starvation. The insensitive response of the psi mutant to brefeldin A suggests that LPR1 and PDR2 (Pi Deficiency Response 2) function in opposite ways in regulating the root growth response to Pi starvation in the endoplamic reticulum.
authors.affiliation: State Key Laboratory of Plant Physiology and Biochemistry, College of Life Science, Zhejiang University, Hangzhou, 310058, PR China.
authors.forename: Xuemin
authors.initials: X
authors.lastname: Wang
authors.forename: Guankui
authors.initials: G
authors.lastname: Du
authors.forename: Xuming
authors.initials: X
authors.lastname: Wang
authors.forename: Yijun
authors.initials: Y
authors.lastname: Meng
authors.forename: Yiyi
authors.initials: Y
authors.lastname: Li
authors.forename: Ping
authors.initials: P
authors.lastname: Wu
authors.forename: Keke
authors.initials: K
authors.lastname: Yi
mesh_terms: D017360:Arabidopsis / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004721:Endoplasmic Reticulum / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D007210:Indoleacetic Acids / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D009154:Mutation; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D018517:Plant Roots / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism; D011401:Promoter Regions, Genetic; D018749:RNA, Plant / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; D007210:Indoleacetic Acids; D010710:Phosphates; D018749:RNA, Plant; C543910:LPR1 protein, Arabidopsis; D010088:Oxidoreductases; D008025:Ligases; C502552:SIZ1 protein, Arabidopsis