Examples of histidine kinase in the following topics:
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- Signal transduction occurs through the transfer of phosphoryl groups from adenosine triphosphate (ATP) to a specific histidine residue in the histidine kinases (HK).
- Subsequently the histidine kinase catalyzes the transfer of the phosphate group on the phosphorylated histidine residues to an aspartic acid residue on the response regulator (RR).
- Signal transducing histidine kinases are the key elements in two-component signal transduction systems.
- Examples of histidine kinases are EnvZ, which plays a central role in osmoregulation, and CheA, which plays a central role in the chemotaxis system.
- Histidine kinases usually have an N-terminal ligand-binding domain and a C-terminal kinase domain, but other domains may also be present.
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- The activation of the receptor by an external stimulus causes autophosphorylation in the histidine kinase, CheA, at a single highly-conserved histidine residue.
- CheA in turn transfers phosphoryl groups to conserved aspartate residues in the response regulators CheB and CheY [note: CheA is a histidine kinase and it does not actively transfer the phosphoryl group.
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- STAT activation initiates the most well-defined cell signaling pathway for all IFNs, the classical Janus kinase-STAT (JAK-STAT) signaling pathway.
- Type I IFNs further activate p38 mitogen-activated protein kinase (MAP kinase) to induce gene transcription.
- Antiviral and antiproliferative effects specific to type I IFNs result from p38 MAP kinase signaling.
- The phosphatidylinositol 3-kinase (PI3K) signaling pathway is also regulated by both type I and type II IFNs.
- PI3K activates P70-S6 Kinase 1, an enzyme that increases protein synthesis and cell proliferation; phosphorylates of ribosomal protein s6, which is involved in protein synthesis; and phosphorylates a translational repressor protein called eukaryotic translation-initiation factor 4E-binding protein 1 (EIF4EBP1) in order to deactivate it.
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- Its antiviral activity requires phosphorylation by the HCMV protein kinase, pUL97.
- HCMV drugs have been designed to target the virus' DNA polymerase (pUL54), protein kinase (pUL97), and cellular kinases.
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- His-tag, 5-10 histidines bound by a nickel or cobalt chelate (HHHHHH)
- Eighteen bases coding six histidines are inserted right after the START codon or right before the STOP codon.
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- The adapter proteins and kinases that mediate TLR signaling have also been targeted.
- IRAK kinases then phosphorylate and activate the protein TRAF6, which in turn polyubiquinates the protein TAK1, as well as itself in order to facilitate binding to IKKβ.
- TRIF activates the kinases TBK1 and RIP1, which creates a branch in the signaling pathway.
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- This tag could be histidine (His) tag or any other marker peptide.
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- This ADP-ribosylation involves the transfer of an ADP-ribose from NAD+ to a diphthamide (a modified histidine) residue within the EF-2 protein.
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- These peptides include two or more positively charged residues provided by arginine, lysine or, in acidic environments, histidine, and a large proportion (generally >50%) of hydrophobic residues.
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- Also, they induce activation of several signal transduction cascades, including activation of PI-3 kinase.