title: Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein.
abstract: ATP-binding cassette (ABC) systems belong to a large superfamily of proteins that couple the energy released from ATP hydrolysis to a wide variety of cellular processes, including not only transport of various molecules, but also gene regulation, and DNA repair. Mutations in the bacterial uup gene, which encodes a cytosolic ABC ATPase, lead to an increase in the frequency of precise excision of transposons Tn10 and Tn5, suggesting a role of the Uup protein in DNA metabolism. Uup is a 72 kDa polypeptide which comprises two ABC domains, separated by a 75-residue linker, and a C-terminal domain (CTD) of unknown function. The Uup protein from Escherichia coli has been shown to bind DNA in vitro, and the CTD domain contributes to the DNA-binding affinity. We have produced and purified uniformly labeled (15)N- and (15)N/(13)C Uup CTD domain (region 528-635), and assigned backbone and side-chains resonances using heteronuclear NMR spectroscopy. Secondary structure evaluation based on backbone chemical shifts is consistent with the presence of three α-helices, including two long ones (residues 564-590 and 601-632), suggesting that Uup CTD may fold as an intramolecular coiled coil motif. This work provides the starting point towards determining the first atomic structure of a non-ATPase domain within the vast REG subfamily of ABC soluble ATPases.
authors.affiliation: Laboratoire des BioMolécules UMR 7203, UPMC Université Paris 06, 4 place Jussieu, 75005 Paris, France. ludovic.carlier@upmc.fr
authors.forename: Ludovic
authors.initials: L
authors.lastname: Carlier
authors.forename: A Sander
authors.initials: AS
authors.lastname: Haase
authors.forename: Monica Y
authors.initials: MY
authors.lastname: Burgos Zepeda
authors.forename: Elie
authors.initials: E
authors.lastname: Dassa
authors.forename: Olivier
authors.initials: O
authors.lastname: Lequin
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D018528:ATP-Binding Cassette Transporters; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C105795:Uup protein, E coli