Selected BTB/POZ‐kelch proteins bind ATP

FEBS Letters

De Corte, Veerle¹  Vandekerckhove, Joël¹  Devriendt, Liesbeth¹  Gettemans, Jan¹  T'Jampens, Davy¹ 

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

关键词: Bric-à-brac;    tramtrack;    broad-complex;    Poxvirus zinc finger;    ATP;    5′-p-Fluorosulfonyl-benzoyl-adenosine;    Modification;    Kelch;    AFK;    actin-fragmin kinase;    BTB/POZ;    bric-à-brac;    tramtrack;    broad-complex/Poxvirus zinc fingers;    CKR;    Caenorhabditis elegans kelch related;    FSBA;    5′-p-fluorosulfonyl-benzoyl-adenosine;    PMSF;    phenylmethylsulfonyl fluoride;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(02)02456-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown