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Eukaryotes have "two-component" signal transducers

C Chang1, E M Meyerowitz

  • 1156-29 Biology Division, California Institute of Technology, Pasadena 91125.

Research in Microbiology
|June 1, 1994
PubMed
Summary
This summary is machine-generated.

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Eukaryotic proteins share sequence features with prokaryotic two-component signal transducers. Their functions and signal identities remain largely unknown, suggesting novel signaling mechanisms.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Biochemistry

Background:

  • Eukaryotic proteins exhibit sequence similarities to prokaryotic two-component signal transducer systems.
  • Key domains like histidine phosphotransfer (HPK) and receiver domains are present in some eukaryotic proteins (e.g., ETR1, Sln1).
  • Other eukaryotic proteins (phytochromes, BCKDH kinase, dr6) show distant relationships, with less conserved motifs.

Purpose of the Study:

  • To investigate the relationship between eukaryotic proteins and prokaryotic two-component signal transducer families.
  • To explore the diversity in domain arrangements within these families.
  • To identify potential novel signaling pathways in eukaryotes.

Main Methods:

  • Comparative sequence analysis of eukaryotic and prokaryotic proteins.

Related Experiment Videos

  • Identification of conserved motifs and domain architectures.
  • Functional domain analysis.

    • Main Results:

    • Eukaryotic proteins like ETR1 and Sln1 possess putative HPK and receiver domains, similar to prokaryotic systems.
    • Domain arrangements vary, with components within the same protein or on separate proteins.
    • BCKDH kinase, despite a known function, phosphorylates a non-orthodox substrate at serine residues.

    Conclusions:

    • Eukaryotic proteins represent new members of the two-component signal transducer family, expanding its known diversity.
    • The precise functions and transduced signals for most of these eukaryotic proteins are yet to be elucidated.
    • Eukaryotic two-component modules may operate through novel mechanisms or in conjunction with different signaling components.