Possible His to Asp phosphorelay signaling in an Arabidopsis two‐component system

FEBS Letters

Urao, Takeshi¹  Yamaguchi-Shinozaki, Kazuko¹  Miyata, Shinichi¹  Shinozaki, Kazuo² 

[1] Biological Resources Division, Japan International Research Center for Agricultural Science (JIRCAS), Ministry of Agriculture, Forestry and Fisheries, 1-2 Ohwashi, Tsukuba, Ibaraki 305-8686, Japan,;Laboratory of Plant Molecular Biology, Institute of Physical and Chemical Research (RIKEN), Tsukuba Life Science Center, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan

关键词: Histidine kinase;    Histidine-containing phosphotransfer domain;    Protein–protein interaction;    Response regulator;    Two-component system;    Yeast two-hybrid analysis;    Arabidopsis thaliana;   

DOI  :  10.1016/S0014-5793(00)01860-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have so far cloned a cDNA encoding a hybrid-type histidine kinase (ATHK1), three cDNAs encoding phosphorelay intermediates (ATHP1–3), and four cDNAs encoding response regulators (ATRR1–4) from Arabidopsis thaliana. To determine which molecules constitute a His to Asp phosphorelay pathway, we examined protein–protein interactions between them using a pairwise yeast two-hybrid analysis, as an initial step. We detected a specific interaction between ATHK1 and ATHP1. We further examined protein–protein interactions between ATHP1–3 and other histidine kinases. We detected interactions between ETR1 and all ATHPs, and between CKI1 and ATHP1 or ATHP2. Interestingly, ERS1 could not interact with any ATHPs. We also examined protein–protein interactions between ATHP1-3 and ATRR1-4. The results indicated that ATHP2 could interact with ATRR4, and that ATHP3 could interact with ATRR1 or ATRR4. However, ATHP1 could not interact with any ATRRs. On the basis of these results, we discuss the possible phosphorelay networks in an Arabidopsis two-component system.

【 授权许可】

Unknown