title: A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803.
abstract: Despite significant progress in clarifying the subunit compositions and functions of the multiple NDH-1 complexes in cyanobacteria, the assembly factors and their roles in assembling these NDH-1 complexes remain elusive. Two mutants sensitive to high light for growth and impaired in NDH-1-dependent cyclic electron transport around photosystem I were isolated from Synechocystis sp. strain PCC 6803 transformed with a transposon-tagged library. Both mutants were tagged in the ssl3829 gene encoding an unknown protein, which shares significant similarity with Arabidopsis (Arabidopsis thaliana) CHLORORESPIRATORY REDUCTION7. The ssl3829 product was localized in the cytoplasm and associates with an NDH-1 hydrophilic arm assembly intermediate (NAI) of about 300 kD (NAI300) and an NdhI maturation factor, Slr1097. Upon deletion of Ssl3829, the NAI300 complex was no longer visible on gels, thereby impeding the assembly of the NDH-1 hydrophilic arm. The deletion also abolished Slr1097 and consequently reduced the amount of mature NdhI in the cytoplasm, which repressed the dynamic assembly process of the NDH-1 hydrophilic arm because mature NdhI was essential to stabilize all functional NAIs. Therefore, Ssl3829 plays an important role in the assembly of the NDH-1 hydrophilic arm by accumulating the NAI300 complex and Slr1097 protein in the cytoplasm.
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.).
authors.forename: Xiaozhuo
authors.initials: X
authors.lastname: Wang
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.).
authors.forename: Fudan
authors.identifier: 0000-0002-8882-5968
authors.initials: F
authors.lastname: Gao
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.).
authors.forename: Jingsong
authors.identifier: 0000-0002-8044-7608
authors.initials: J
authors.lastname: Zhang
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.).
authors.forename: Jiaohong
authors.initials: J
authors.lastname: Zhao
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.).
authors.forename: Teruo
authors.identifier: 0000-0001-6061-8273
authors.initials: T
authors.lastname: Ogawa
authors.affiliation: College of Life and Environment Sciences, Shanghai Normal University, Shanghai 200234, China (X.W., F.G., Jin.Z., Jia.Z., W.M.); andBioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan (T.O.) wma@shnu.edu.cn.
authors.forename: Weimin
authors.identifier: 0000-0003-4964-415X
authors.initials: W
authors.lastname: Ma
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004579:Electron Transport; D057927:Hydrophobic and Hydrophilic Interactions; D008027:Light; D008954:Models, Biological; D009154:Mutation; D045331:Photosystem I Protein Complex / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits; D017384:Sequence Deletion; D046939:Synechocystis / Q000235:genetics* / Q000378:metabolism / Q000528:radiation effects
chemical_list: D001426:Bacterial Proteins; D045331:Photosystem I Protein Complex; D021122:Protein Subunits