Identification of Interacting Motifs Between Armadillo Repeat Containing 1 (ARC1) and Exocyst 70 A1 (Exo70A1) Proteins in Brassica oleracea

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• 作者：Jing Liu ; Hecui Zhang ; Xiaoping Lian ; Richard Converse ; Liquan Zhu
• 关键词：Brassica oleracea ; Armadillo repeat containing 1 ; Exocyst 70 A1 ; Recognition motif ; Interaction
• 刊名：The Protein Journal
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：35
• 期：1
• 页码：34-43
• 全文大小：1,269 KB
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• 作者单位：Jing Liu (1)
  Hecui Zhang (1)
  Xiaoping Lian (2)
  Richard Converse (3)
  Liquan Zhu (1)
  
  1. College of Agronomy and Biotechnology, Southwest University, Chongqing, 400716, China
  2. College of Horticulture and Landscape Architecture, Southwest University, Chongqing, 400716, China
  3. Department of Biological Sciences, University of Cincinnati, Cincinnati, OH, 45267-0524, USA
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Bioorganic Chemistry
  Biochemistry
  Organic Chemistry
  Animal Anatomy, Morphology and Histology
  
• 出版者：Springer Netherlands
• ISSN：1573-4943

文摘

In order to identify the functional domains which regulate the interaction between the self-incompatibility proteins armadillo repeat containing 1 (ARC1) and exocyst 70 A1 (Exo70A1) in Brassica oleracea, fragments containing selected motifs of ARC1 (ARC1₂₁₀, ARC1₂₄₆, ARC1₂₇₉, ARC1₃₅₄) and site-specific mutants with substitutions at possible interaction sites (ARC1_354m, ARC1_664m) were PCR amplified and inserted into pGADT7, while coding sequences from Exo70A1 (Exo70A1₈₅, Exo70A1) were subcloned into pGBKT7. The interactions between the protein products produced by these constructs were then analyzed utilizing a yeast two-hybrid system. Our data indicate that both ARC1₂₁₀ and ARC1₂₄₆ interact strongly with Exo70A1₈₅ and Exo70A1, while ARC1₂₇₉, ARC1₃₅₄, ARC1_354m and ARC1_664m exhibited a weak interaction, indicating that the recognition sites are located within the 210 N-terminal amino acids of ARC1 and the 85 N-terminal amino acids of Exo70A1. This was further verified by GST pull-down analysis. This supports a model in which the N-terminal leucine zipper of ARC1 and the first 85 N-terminal amino acids of Exo70A1 mediate the interaction between these two proteins. Bioinformatic and phylogenetic analysis demonstrated that these motifs were highly conserved across different species, indicating that the interaction characterized in B. oleracea may operate in a wide array of cultivars. Keywords Brassica oleracea Armadillo repeat containing 1 Exocyst 70 A1 Recognition motif Interaction