Receiver domain of sensor histidine kinase CKI1: Difference between revisions

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Tomas Klumpler, Jaime Prilusky, Michal Harel, Alexander Berchansky

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 == Biological Function ==
-'''CKI1 as member of Multistep phosphorelay signaling in ''Arabidopsis'''''
+'''CKI1 as member of Multistep phosphorelay signaling in ''Arabidopsis'''''<br />
 The sensor histidine kinase CKI1 was identified as an activator of a cytokinin-like response when overexpressed in hypocotyl explants <ref>PMID:8875940</ref> and it is essential for the female gametophyte development<ref>PMID:12426401</ref><ref>PMID:12774227</ref>. Cytokinin response in ''Arabidopsis'' involves shoot and root growth regulation, leaf senesce, circadian rhythms etc <ref>PMID:22639635</ref>. No cytokinin binding to CKI1 has been detected, and in contrast to the genuine cytokinin receptors of ''Arabidopsis'', CKI1 was found to be constitutively active in bacteria and yeast or ''Arabidopsis'' protoplasts<ref>PMID:11577198</ref><ref>PMID:11574878</ref>.
 Cytokinin signalling in plants is triggered by MSP<ref>PMID:10664616</ref> , which was adopted by plants from bacterial Two-component system<ref>PMID:12226482</ref>. The signalling molecule is bound to the sensory histidin-kinase and then is transferred via AHPs (AHP1-AHP5) to nuclear response regulators (ARRs). ARRs act as transcription factors or interact with other effector proteins<ref>PMID:12972049</ref> to perform specific cellular response to initial environmental stimuli. In contrast to ancestral Two-component signalling in bacteria, protein interactions in plant MSP are supposed to be rather nonspecific. The current MSP interaction maps from ''Arabidopsis'' are based on yeast two-hybrid system<ref>PMID:10930573</ref><ref>PMID:    16965536</ref><ref>PMID:18642946</ref> and show the AHPs as highly promiscuous, able to interact with all cytokinin receptors, number of other histidine-kinases and number of ARRs.
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 The crystal structure of CKI1RD shows the conformational conservation of RDs belonging to CheY-like protein superfamily <ref>PMID:8257674</ref><ref>PMID:19036790</ref>. CKI1RD is folded in a (α/β)5 manner with central β-sheet formed from parallel beta-strands (β2-β1-β3-β4-β5) surrounded on both sides by two (α1 and α5) and three (α2, α3, α4) α-helices. Secondary structure elements are connected by five loops L1-L5 on the face side of the protein. The active site with phosphoacceptor D1050 is located at the C-termini of the central β3-strand in a pocket delineated loops L1, L3 and L5. A highly conserved triad of carboxyl oxygens formed by D1050 together with D992 and D993 and carbonyl oxygen of Q1052 give the active site an acidic character. This architecture of the active site is well conserved among CheY-like superfamily and corresponds to the phosphotransfer function of the receiver domains.
 The octahedral coordination geometry of magnesium ion in this crystal is not complete. Magnesium ion is four-coordinated with carboxyl oxygens of D993 and D1050, carbonyl oxygen of Q1052 and with one water molecule that forms a hydrogen bridge to the carboxyl oxygen of D992.
-Magnesium binding mediates slight structural changes of the active site. Upon magnesium binding, the side chain of the D1050 rotates by app. 90° toward the divalent cation. The connection via salt bridge between D1050 and K1105 induces the rotation of K1105, whereas the salt bridge remains established.
+Magnesium binding mediates slight structural changes of the active site. Upon magnesium binding, the side chain of the D1050 rotates by 90° toward the divalent cation. The connection via salt bridge between D1050 and K1105 induces the rotation of K1105, whereas the salt bridge remains established.
 More, the NMR analysis shows magnesium binding to stabilize conformational flexibility of the loop L3 in the solution<ref>PMID:21569135</ref>.