The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.

PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK, Jaromír MAREK, Radka DOPITOVÁ, Jan HEJÁTKO and Lubomír JANDA. The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity. 1st ed. Suzhou, China: Cold Spring Harbor Conferences Asia, 2010, p. 47.

Basic information

• Original name: The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.
• Authors: PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK, Jaromír MAREK, Radka DOPITOVÁ, Jan HEJÁTKO and Lubomír JANDA.
• Edition: 1. vyd. Suzhou, China, p. 47-47, 2010.
• Publisher: Cold Spring Harbor Conferences Asia

Other information

• Original language: English
• Type of outcome: Proceedings paper
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: China
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Organization unit: Faculty of Science
• Keywords (in Czech): multistep phosphorelay, 3D structure, NMR analysis
• Keywords in English: vícekomponentní fosforylace, 3-D struktura, NMR analýza

Abstract

In Arabidopsis multistep phosphorelay (MSP) signalling, the signal is transferred from sensor histidine kinase (HK) via histidine-containing phosphotransfer proteins (AHP1-5) to nuclear response regulators. In contrast to bacteria, MSP protein interactions in plants are supposed to be rather non-specific. Using both in vivo and in vitro assays we have found that the C-terminal receiver domain of HK CKI1 (CKI1RD) interacts with AHP2, 3 and 5 with different affinities. We determined crystal structure of free CKI1RD and CKI1RD in a complex with Mg2+. We have found that CKI1RD shares a particular similarity with the only known structure of plant HK, ETR1RD, with the main differences in the loop 3. Structural dynamics of CKIRD in solution was studied in detail by NMR in the absence or presence of Mg2+ that was shown to be indispensable to the transphosphorylation activity and BeF3-, the isomorphous stable phosphate analogue. Finally, using in vitro assay (indirect ELISA) we have found, that presence of Mg2+ and acetyl phosphate on one side and BeF3- on the other one affects the interaction of CKI1RD with its downstream signalling partners and may modulate AHP binding specificity in MSP signalling. Observed structural changes, their dynamics and potential influence on signal transduction specificity via MSP in plants will be discussed in detail.

Links

• GA521/09/1699, research and development project: Name: Imunomodulace jako nástroj funkční proteomiky při studiu cytokininové signální dráhy u Arabidopsis thaliana

Investor: Czech Science Foundation, Immunomodulation as a functional proteomics tool for cytokinin signaling study in Arabidopsis thaliana

• LC06034, research and development project: Name: Regulace morfogeneze rostlinných buněk a orgánů

Investor: Ministry of Education, Youth and Sports of the CR, Regulation of morphogenesis of plant cells and organs

• MSM0021622413, plan (intention): Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

• MSM0021622415, plan (intention): Name: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations