title: Selected BTB/POZ-kelch proteins bind ATP.
abstract: 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.
authors.affiliation: Flanders Interuniversity Institute for Biotechnology (V.I.B.), Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Baertsoenkaai 3, B-9000, Ghent, Belgium.
authors.forename: Davy
authors.initials: D
authors.lastname: T'Jampens
authors.forename: Liesbeth
authors.initials: L
authors.lastname: Devriendt
authors.forename: Veerle
authors.initials: V
authors.lastname: De Corte
authors.forename: Joël
authors.initials: J
authors.lastname: Vandekerckhove
authors.forename: Jan
authors.initials: J
authors.lastname: Gettemans
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary / Q000235:genetics; D006801:Humans; D000072019:Kelch-Like ECH-Associated Protein 1; D051379:Mice; D008840:Microfilament Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins; D016839:Physarum polycephalum / Q000201:enzymology / Q000235:genetics; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
chemical_list: C402243:ABTB1 protein, human; C509774:Abtb1 protein, mouse; D048868:Adaptor Proteins, Signal Transducing; D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; C485646:KLHL2 protein, human; C117301:Keap1 protein, mouse; D000072019:Kelch-Like ECH-Associated Protein 1; C120754:Klhl2 protein, mouse; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D000255:Adenosine Triphosphate; C074377:actin kinase; D017346:Protein Serine-Threonine Kinases