About: Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
rdfs:seeAlso
Description
  • Multistep phosphorelay (MSP) signaling mediates responses to a variety of important stimuli in plants. In Arabidopsis MSP, the signal is transferred from sensor histidine kinase (HK) via histidine phosphotransfer proteins (AHP1–AHP5) to nuclear response regulators. In contrast to ancestral two-component signaling in bacteria, protein interactions in plant MSP are supposed to be rather nonspecific. Here, we show that the C-terminal receiver domain of HK CKI1 (CKI1RD) is responsible for the recognition of CKI1 downstream signaling partners, and specifically interacts with AHP2, AHP3 and AHP5 with different affinities. We studied the effects of Mg2+, the co-factor necessary for signal transduction via MSP, and phosphorylation-mimicking BeF3 ) on CKI1RD in solution, and determined the crystal structure of free CKI1RD and CKI1RD in a complex with Mg2+. We found that the structure of CKI1RD shares similarities with the only known structure of plant HK, ETR1RD, with the main differences being in loop L3.
  • Multistep phosphorelay (MSP) signaling mediates responses to a variety of important stimuli in plants. In Arabidopsis MSP, the signal is transferred from sensor histidine kinase (HK) via histidine phosphotransfer proteins (AHP1–AHP5) to nuclear response regulators. In contrast to ancestral two-component signaling in bacteria, protein interactions in plant MSP are supposed to be rather nonspecific. Here, we show that the C-terminal receiver domain of HK CKI1 (CKI1RD) is responsible for the recognition of CKI1 downstream signaling partners, and specifically interacts with AHP2, AHP3 and AHP5 with different affinities. We studied the effects of Mg2+, the co-factor necessary for signal transduction via MSP, and phosphorylation-mimicking BeF3 ) on CKI1RD in solution, and determined the crystal structure of free CKI1RD and CKI1RD in a complex with Mg2+. We found that the structure of CKI1RD shares similarities with the only known structure of plant HK, ETR1RD, with the main differences being in loop L3. (en)
Title
  • Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
  • Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. (en)
skos:prefLabel
  • Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.
  • Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. (en)
skos:notation
  • RIV/00216224:14740/11:00050106!RIV12-GA0-14740___
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(ED1.1.00/02.0068), P(GA521/09/1699), P(GAP305/11/0756), P(GD204/08/H054), P(LC06034), S, Z(MSM0021622413), Z(MSM0021622415)
http://linked.open...iv/cisloPeriodika
  • 5
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 232767
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14740/11:00050106
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • multistep phosphorelay; receiver domain; CKI1; crystal structure; NMR spectroscopy; Arabidopsis thaliana (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [DDB1964A95F5]
http://linked.open...i/riv/nazevZdroje
  • The Plant Journal
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 67
http://linked.open...iv/tvurceVysledku
  • Dopitová, Radka
  • Hejátko, Jan
  • Horák, Jakub
  • Janda, Lubomír
  • Marek, Jaromír
  • Papoušková, Veronika
  • Sklenář, Vladimír
  • Žídek, Lukáš
  • Pekárová, Blanka
  • Borkovcová, Petra
  • Jansen, Séverine
  • Klumpler, Tomáš
  • Nejedlá, Eliška
  • Třísková, Olga
http://linked.open...ain/vavai/riv/wos
  • 000294827700008
http://linked.open...n/vavai/riv/zamer
issn
  • 0960-7412
number of pages
http://bibframe.org/vocab/doi
  • 10.1111/j.1365-313X.2011.04637.x
http://localhost/t...ganizacniJednotka
  • 14740
is http://linked.open...avai/riv/vysledek of
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software