title: Tomato SlSnRK1 protein interacts with and phosphorylates βC1, a pathogenesis protein encoded by a geminivirus β-satellite.
abstract: The βC1 protein of tomato yellow leaf curl China β-satellite functions as a pathogenicity determinant. To better understand the molecular basis of βC1 in pathogenicity, a yeast two-hybrid screen of a tomato (Solanum lycopersicum) cDNA library was carried out using βC1 as bait. βC1 interacted with a tomato SUCROSE-NONFERMENTING1-related kinase designated as SlSnRK1. Their interaction was confirmed using a bimolecular fluorescence complementation assay in Nicotiana benthamiana cells. Plants overexpressing SnRK1 were delayed for symptom appearance and contained lower levels of viral and satellite DNA, while plants silenced for SnRK1 expression developed symptoms earlier and accumulated higher levels of viral DNA. In vitro kinase assays showed that βC1 is phosphorylated by SlSnRK1 mainly on serine at position 33 and threonine at position 78. Plants infected with βC1 mutants containing phosphorylation-mimic aspartate residues in place of serine-33 and/or threonine-78 displayed delayed and attenuated symptoms and accumulated lower levels of viral DNA, while plants infected with phosphorylation-negative alanine mutants contained higher levels of viral DNA. These results suggested that the SlSnRK1 protein attenuates geminivirus infection by interacting with and phosphorylating the βC1 protein.
authors: State Key Laboratory of Rice Biology, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, People's Republic of China.
authors: Qingtang
authors: Q
authors: Shen
authors: Zhou
authors: Z
authors: Liu
authors: Fengming
authors: F
authors: Song
authors: Qi
authors: Q
authors: Xie
authors: Linda
authors: L
authors: Hanley-Bowdoin
authors: Xueping
authors: X
authors: Zhou
mesh_terms: D004279:DNA, Viral / Q000378:metabolism; D017791:Geminiviridae / Q000378:metabolism / Q000472:pathogenicity*; D018506:Gene Expression Regulation, Plant; D018551:Solanum lycopersicum / Q000201:enzymology* / Q000235:genetics / Q000821:virology*; D009154:Mutation / Q000235:genetics; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D010935:Plant Diseases / Q000821:virology; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D012526:Satellite Viruses / Q000378:metabolism / Q000472:pathogenicity*; D013347:Subcellular Fractions / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D004279:DNA, Viral; D010940:Plant Proteins; D014764:Viral Proteins; D010769:Phosphothreonine; D010768:Phosphoserine