The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured

Marco Nardini, Dmitri Svergun, Peter V Konarev, Stefania Spanò, Mauro Fasano, Chiara Bracco, Alessandra Pesce, Alessandra Donadini, Claudia Cericola, Francesco Secundo, Alberto Luini, Daniela Corda, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)

Abstract

C-terminal binding proteins (CtBPs) are moonlighting proteins involved in nuclear transcriptional corepression and in Golgi membrane tubule fission. Structural information on CtBPs is available for their substrate-binding domain, responsible for transcriptional repressor recognition/binding, and for the nucleotide-binding domain, involved in NAD(H)-binding and dimerization. On the contrary, little is known about the structure of CtBP C-terminal region ( approximately 90 residues), hosting sites for post-translational modifications. In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains. The flexible nature of this protein region, and its structural transitions, may be instrumental for CtBP recognition and binding to diverse molecular partners.
Original languageEnglish
Pages (from-to)1042-50
Number of pages9
JournalProtein science : a publication of the Protein Society
Volume15
Issue number5
DOIs
Publication statusPublished - May 2006

Keywords

  • Alcohol Oxidoreductases
  • Amino Acid Sequence
  • Binding Sites
  • Circular Dichroism
  • DNA-Binding Proteins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoproteins
  • Protein Folding
  • Repressor Proteins
  • Transcription Factors
  • Transcription, Genetic

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