NMR analyses of the receiver domain of CKI1 histidine kinase
and its interaction with AHP proteins

a 2009

NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

PEKÁROVÁ, Blanka; Olga TŘÍSKOVÁ; Lukáš ŽÍDEK; Jaromír MAREK; Jakub HORÁK et. al.

Základní údaje

Originální název

NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins

Autoři

PEKÁROVÁ, Blanka (203 Česká republika); Olga TŘÍSKOVÁ (203 Česká republika); Lukáš ŽÍDEK (203 Česká republika); Jaromír MAREK (203 Česká republika); Jakub HORÁK (203 Česká republika); Radka DOPITOVÁ (203 Česká republika); Jan HEJÁTKO (203 Česká republika, garant) a Lubomír JANDA (203 Česká republika)

Vydání

ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium, 2009

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

Genetika a molekulární biologie

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14310/09:00039607

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Histidine Kinase; CKI1; receiver domain; AHP proteins

Změněno: 9. 4. 2010 15:01, Mgr. Radka Dopitová, Ph.D.

Anotace

V originále

In a multistep phosphorelay, the C-terminal receiver domain of sensor histidine kinases is supposed to be involved in protein-protein interactions with its downstream signalling partners, the AHP proteins. Here we show that CKI1RD interacts in vivo and in vitro with AHP2, 3, and 5 with different affinities. To understand protein-protein interactions on the molecular level, the structure of CKI1RD in solution has been studied in details by nuclear magnetic resonance (NMR). Effects of magnesium ions (Mg2+) and phosphate analogue beryllium fluoride on chemical shift changes of CKI1RD have been studied in a series of titration experiments and the most significantly affected residues were identified. Observed chemical shift changes were mapped on a solved crystallographic structure of the protein. Molecular motions were investigated by NMR relaxation experiments with free, Mg2+-bound, and beryllofluorinated CKI1RD. Based on these data and in combination with bioinformatics approach, we determined four regions that might be responsible for the observed specificity of protein-protein interactions between CKI1RD and individual AHP proteins.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

LC06034, projekt VaV

Název: Regulace morfogeneze rostlinných buněk a orgánů

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Regulace morfogeneze rostlinných buněk a orgánů

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

MSM0021622415, záměr

Název: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Molekulární podstata buněčných a tkáňových regulací

Citovat

PEKÁROVÁ, Blanka; Olga TŘÍSKOVÁ; Lukáš ŽÍDEK; Jaromír MAREK; Jakub HORÁK; Radka DOPITOVÁ; Jan HEJÁTKO a Lubomír JANDA. NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins. In ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium. 2009.

@proceedings{877331,
   author = {Pekárová, Blanka and Třísková, Olga and Žídek, Lukáš and Marek, Jaromír and Horák, Jakub and Dopitová, Radka and Hejátko, Jan and Janda, Lubomír},
   booktitle = {ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium},
   keywords = {Histidine Kinase; CKI1; receiver domain; AHP proteins},
   language = {eng},
   title = {NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins},
   url = {http://acpd.cas.cz/wp-content/uploads/2009/06/ACPD2009_Book_of_Abstracts.pdf},
   year = {2009}
}

TY  - CONF
ID  - 877331
AU  - Pekárová, Blanka - Třísková, Olga - Žídek, Lukáš - Marek, Jaromír - Horák, Jakub - Dopitová, Radka - Hejátko, Jan - Janda, Lubomír
PY  - 2009
TI  - NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins
KW  - Histidine Kinase
KW  - CKI1
KW  - receiver domain
KW  - AHP proteins
UR  - http://acpd.cas.cz/wp-content/uploads/2009/06/ACPD2009_Book_of_Abstracts.pdf
N2  - In a multistep phosphorelay, the C-terminal receiver domain of sensor histidine kinases is supposed to be involved in protein-protein interactions with its downstream signalling partners, the AHP proteins. Here we show that CKI1RD interacts in vivo and in vitro with AHP2, 3, and 5 with different affinities. To understand protein-protein interactions on the molecular level, the structure of CKI1RD in solution has been studied in details by nuclear magnetic resonance (NMR). Effects of magnesium ions (Mg2+) and phosphate analogue beryllium fluoride on chemical shift changes of CKI1RD have been studied in a series of titration experiments and the most significantly affected residues were identified. Observed chemical shift changes were mapped on a solved crystallographic structure of the protein. Molecular motions were investigated by NMR relaxation experiments with free, Mg2+-bound, and beryllofluorinated CKI1RD. Based on these data and in combination with bioinformatics approach, we determined four regions that might be responsible for the observed specificity of protein-protein interactions between CKI1RD and individual AHP proteins.
ER  -

PEKÁROVÁ, Blanka; Olga TŘÍSKOVÁ; Lukáš ŽÍDEK; Jaromír MAREK; Jakub HORÁK; Radka DOPITOVÁ; Jan HEJÁTKO a Lubomír JANDA. NMR analyses of the receiver domain of CKI1 histidine kinase and its interaction with AHP proteins. In \textit{ACPD 2009 : Auxins and Cytokinins in Plant Development International Symposium}. 2009.

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