title: CaM/BAG5/Hsc70 signaling complex dynamically regulates leaf senescence.
abstract: Calcium signaling plays an essential role in plant cell physiology, and chaperone-mediated protein folding directly regulates plant programmed cell death. The Arabidopsis thaliana protein AtBAG5 (Bcl-2-associated athanogene 5) is unique in that it contains both a BAG domain capable of binding Hsc70 (Heat shock cognate protein 70) and a characteristic IQ motif that is specific for Ca(2+)-free CaM (Calmodulin) binding and hence acts as a hub linking calcium signaling and the chaperone system. Here, we determined crystal structures of AtBAG5 alone and in complex with Ca(2+)-free CaM. Structural and biochemical studies revealed that Ca(2+)-free CaM and Hsc70 bind AtBAG5 independently, whereas Ca(2+)-saturated CaM and Hsc70 bind AtBAG5 with negative cooperativity. Further in vivo studies confirmed that AtBAG5 localizes to mitochondria and that its overexpression leads to leaf senescence symptoms including decreased chlorophyll retention and massive ROS production in dark-induced plants. Mutants interfering the CaM/AtBAG5/Hsc70 complex formation leads to different phenotype of leaf senescence. Collectively, we propose that the CaM/AtBAG5/Hsc70 signaling complex plays an important role in regulating plant senescence.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.|College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Luhua
authors.initials: L
authors.lastname: Li
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.|College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Yangfei
authors.initials: Y
authors.lastname: Xing
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.|College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Dong
authors.initials: D
authors.lastname: Chang
authors.affiliation: College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Shasha
authors.initials: S
authors.lastname: Fang
authors.affiliation: College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Boyang
authors.initials: B
authors.lastname: Cui
authors.affiliation: College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Li
authors.affiliation: College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Xuejie
authors.initials: X
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Shang
authors.initials: S
authors.lastname: Guo
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Xue
authors.initials: X
authors.lastname: Yang
authors.affiliation: College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Shuzhen
authors.initials: S
authors.lastname: Men
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China.|College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.|Synergetic Innovation Center of Chemical Science and Engineering, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Yuequan
authors.initials: Y
authors.lastname: Shen
mesh_terms: D017360:Arabidopsis / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D050883:HSC70 Heat-Shock Proteins / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D018515:Plant Leaves / Q000502:physiology*; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; C000627099:BAG5 protein, Arabidopsis; D002147:Calmodulin; D050883:HSC70 Heat-Shock Proteins; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D010940:Plant Proteins