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Selected BTB/POZ‐kelch proteins bind ATP
Author(s) -
T'Jampens Davy,
Devriendt Liesbeth,
De Corte Veerle,
Vandekerckhove Joël,
Gettemans Jan
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02456-0
Subject(s) - binding domain , microbiology and biotechnology , biochemistry , actin , chemistry , biology , binding site
Proteins with a bric‐à‐brac, tramtrack, broad‐complex/Poxvirus zinc fingers (BTB/POZ) domain are implicated in a broad variety of biological processes, including DNA binding, regulation of gene transcription and organization of macromolecular structures. Kelch domain containing BTB/POZ proteins like Mayven and Keap1 display limited sequence similarity with the actin‐fragmin kinase from Physarum , a protein kinase with a kelch domain. We show that mouse Keap1, a Caenorhabditis elegans protein that we named CKR, and human Mayven bind 5′‐ p ‐fluorosulfonyl‐benzoyl‐adenosine (FSBA), a covalently modifying ATP analogue. Binding with 2‐azido‐ATP or ATP‐Sepharose is also demonstrated. In contrast to Mayven, FSBA binding by CKR and Keap1 was specifically inhibited by excess ATP. The ATP binding pocket is located in the N‐terminal half of Keap1. Our findings indicate that several, but not all, BTB/POZ‐kelch domain proteins possess an inconspicuous ATP binding cassette.