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Related Experiment Videos

Selected BTB/POZ-kelch proteins bind ATP.

Davy T'Jampens1, Liesbeth Devriendt, Veerle De Corte

  • 1Flanders Interuniversity Institute for Biotechnology (V.I.B.), Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Baertsoenkaai 3, B-9000, Ghent, Belgium.

FEBS Letters
|April 18, 2002
PubMed
Summary

Several BTB/POZ-kelch proteins, including Keap1 and CKR, bind ATP, suggesting a conserved ATP-binding cassette. This finding reveals a previously unrecognized function for these proteins in cellular processes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • Proteins with Bric-à-brac, Tramtrack, Broad-complex/Poxvirus zinc fingers (BTB/POZ) domains are involved in diverse biological functions.
  • Kelch domain-containing BTB/POZ proteins, such as Mayven and Keap1, share similarities with protein kinases.

Purpose of the Study:

  • To investigate the potential ATP-binding capabilities of specific BTB/POZ-kelch domain proteins.
  • To identify the functional significance of ATP binding in these proteins.

Main Methods:

  • Utilized ATP analogs like 5'-p-fluorosulfonyl-benzoyl-adenosine (FSBA) for covalent modification studies.
  • Employed 2-azido-ATP and ATP-Sepharose for binding assays.
  • Performed competitive inhibition assays with excess ATP to confirm specificity.

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Main Results:

  • Mouse Keap1, Caenorhabditis elegans CKR, and human Mayven demonstrated binding to the ATP analog FSBA.
  • Binding of FSBA to CKR and Keap1 was specifically inhibited by excess ATP, unlike Mayven.
  • The ATP-binding pocket in Keap1 was localized to its N-terminal region.

Conclusions:

  • A subset of BTB/POZ-kelch domain proteins possess an ATP-binding cassette.
  • This suggests a conserved, yet previously unrecognized, role for ATP binding in the function of these proteins.