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

D 2010

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 et. al.

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

Language

English

Type of outcome

Stať ve sborníku

Field of Study

10600 1.6 Biological sciences

Country of publisher

China

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

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

Změněno: 29/4/2011 15:31, RNDr. Lubomír Janda, Ph.D.

Abstract

V originále

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

Citovat

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.

@inproceedings{911185,
   author = {Pekárová, Blanka and Klumpler, Tomáš and Třísková, Olga and Horák, Jakub and Žídek, Lukáš and Marek, Jaromír and Dopitová, Radka and Hejátko, Jan and Janda, Lubomír},
   address = {Suzhou, China},
   edition = {1},
   keywords = {vícekomponentní fosforylace, 3-D struktura, NMR analýza},
   language = {eng},
   location = {Suzhou, China},
   pages = {47-47},
   publisher = {Cold Spring Harbor Conferences Asia},
   title = {The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.},
   url = {http://meetings.cshl.edu/CSHAsia/plants10.html},
   year = {2010}
}

TY  - JOUR
ID  - 911185
AU  - Pekárová, Blanka - Klumpler, Tomáš - Třísková, Olga - Horák, Jakub - Žídek, Lukáš - Marek, Jaromír - Dopitová, Radka - Hejátko, Jan - Janda, Lubomír
PY  - 2010
TI  - The receiver domain of sensor histidine kinase of CKI1: its dynamic structure and binding specificity.
PB  - Cold Spring Harbor Conferences Asia
CY  - Suzhou, China
KW  - vícekomponentní fosforylace, 3-D struktura, NMR analýza
UR  - http://meetings.cshl.edu/CSHAsia/plants10.html
N2  - 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.
ER  -

PEKÁROVÁ, Blanka, Tomáš KLUMPLER, Olga TŘÍSKOVÁ, Jakub HORÁK, Lukáš ŽÍDEK, Jaromír MAREK, Radka DOPITOVÁ, Jan HEJÁTKO and Lubomír JANDA. \textit{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.

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