SUPPRESSOR OF LLP1 1-mediated C-terminal processing is critical for CLE19 peptide activity.
SUPPRESSOR OF LLP1 1-mediated C-terminal processing is critical for CLE19 peptide activity.
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DOI：
10.1111/tpj.12349
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发表时间：
2013-12
期刊：
影响因子：
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通讯作者：
T. Tamaki;S. Betsuyaku;Masayuki Fujiwara;Y. Fukao;H. Fukuda;S. Sawa
中科院分区：
文献类型：
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作者：
T. Tamaki;S. Betsuyaku;Masayuki Fujiwara;Y. Fukao;H. Fukuda;S. Sawa
细胞间的通讯是多细胞生物协调发展的必要条件。CLAVATA3/胚胎周围区相关（CLE）家族的成员是一组小的分泌肽，参与了植物的这些过程。虽然翻译后修饰被认为是其活性不可或缺的，但控制这些修饰的详细机制尚不清楚。在这里，我们报道了LLP1 1的SUPPRESSOR (SOL1)，一种假定的Zn 2 +羧肽酶，以前被分离出来作为CLE19过表达表型的抑制因子，在CLE19蛋白的c端加工中起作用，产生功能性的CLE19肽。新分离的sol1突变体对CLE19过表达具有抗性，这与之前的报道一致（Casamitjana-Martinez， E., Hofhuis, h.f., Xu， J., Liu， C.M, Heidstra， R. and Scheres， B.(2003)）。生物学报，13,1435 -1441)。正如预期的那样，我们使用合成CLE19肽的实验表明，sol1突变本身并不损害CLE信号转导途径。在体外，SOL1具有去除CLE19蛋白c端精氨酸残基的酶活性，而在体内，SOL1依赖的c端精氨酸残基的裂解是CLE19活性的必要条件。此外，SOL1的内体定位表明这种加工发生在分泌途径的内体中。因此，我们的数据表明CLE蛋白的c端加工对于确保CLE活性的重要性。
Cell-to-cell communication is essential for the coordinated development of multicellular organisms. Members of the CLAVATA3/EMBRYO-SURROUNDING REGION-RELATED (CLE) family, a group of small secretory peptides, are involved in these processes in plants. Although post-translational modifications are considered to be indispensable for their activity, the detailed mechanisms governing these modifications are not well understood. Here, we report that SUPPRESSOR OF LLP1 1 (SOL1), a putative Zn²⁺ carboxypeptidase previously isolated as a suppressor of the CLE19 over-expression phenotype, functions in C-terminal processing of the CLE19 proprotein to produce the functional CLE19 peptide. Newly isolated sol1 mutants are resistant to CLE19 over-expression, consistent with the previous report (Casamitjana-Martinez, E., Hofhuis, H.F., Xu, J., Liu, C.M., Heidstra, R. and Scheres, B. (2003) Curr. Biol. 13, 1435-1441). As expected, our experiment using synthetic CLE19 peptide revealed that the sol1 mutation does not compromise CLE signal transduction pathways per se. SOL1 possesses enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. Additionally, the endosomal localization of SOL1 suggests that this processing occurs in endosomes in the secretory pathway. Thus, our data indicate the importance of C-terminal processing of CLE proproteins to ensure CLE activities.