title: Functional analysis of photosystem II in a PsbO-1-deficient mutant in Arabidopsis thaliana.
abstract: The Arabidopsis thaliana mutant psbo1 (formerly the mutant LE18-30), which contains a point mutation in the psbO-1 gene leading to defective expression of the PsbO-1 protein, has recently been described [Murakami, R. et al. (2002) FEBS Lett. 523, 138-142]. This mutant completely lacks the PsbO-1 protein and overexpresses the PsbO-2 protein. To further study the effect of PsbO-1 deficiency on the function of photosystem II, the polyphasic chlorophyll a fluorescence rise and flash fluorescence induction and decay of the relative fluorescence quantum yield were measured in whole leaves from wild type and the psbo1 mutant. Additionally, flash oxygen yield experiments were performed on thylakoid membranes isolated from wild type and the psbo1 mutant. The results obtained indicate that during fluorescence induction the psbo1 gene exhibited an enhanced O to P transition. Additionally, while the J to I transition in wild type accounted for more than 30% of the total fluorescence yield, in the mutant it accounted for less than 2% rise in the total. Analysis of the flash-induced fluorescence rise in the presence of DCMU indicated that in wild type the ratio of PS IIalpha to PS IIbeta reaction centers was approximately 1.2 while in the mutant the ratio was approximately 0.3. Fluorescence decay kinetics in the absence of DCMU indicated that electron transfer to QB was significantly altered in the mutant. Fluorescence decay kinetics in the presence of DCMU indicated that the charge recombination between QA- and the S2 state of the oxygen-evolving complex was retarded. Furthermore, flash oxygen yield analysis indicated that both the S2 and S3 states exhibited significantly longer lifetimes in the psbo1 mutant than in wild type. Our data indicate that while PsbO-1-deficient plants can grow photoautotrophically (although at a reduced growth rate) the photochemistry of PS II is significantly altered.
authors.affiliation: Department of Biological Sciences, Division of Biochemistry and Molecular Biology, Louisiana State University, Baton Rouge, Louisiana 70803, USA.
authors.forename: Haijun
authors.initials: H
authors.lastname: Liu
authors.forename: Laurie K
authors.initials: LK
authors.lastname: Frankel
authors.forename: Terry M
authors.initials: TM
authors.lastname: Bricker
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D052818:Autotrophic Processes / Q000502:physiology; D001665:Binding Sites; D004237:Diuron / Q000494:pharmacology; D006540:Herbicides / Q000494:pharmacology; D010777:Photochemistry; D045332:Photosystem II Protein Complex / Q000235:genetics / Q000378:metabolism*; D018515:Plant Leaves / Q000378:metabolism; D017354:Point Mutation; D011485:Protein Binding; D020524:Thylakoids / Q000737:chemistry / Q000378:metabolism; D013997:Time Factors
chemical_list: D029681:Arabidopsis Proteins; D006540:Herbicides; D045332:Photosystem II Protein Complex; D004237:Diuron