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 journalArticle

32 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

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Co-Repressor Proteins
Protein C
Nucleotides
Circular dichroism spectroscopy
Dimerization
Substrates
Post Translational Protein Processing
Bioinformatics
Circular Dichroism
Computational Biology
X ray scattering
Protein Binding
NAD
C-terminal binding protein
Spectrum Analysis
Proteins
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
X-Rays
Membranes

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

Cite this

Nardini, M., Svergun, D., Konarev, P. V., Spanò, S., Fasano, M., Bracco, C., ... Bolognesi, M. (2006). The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein science : a publication of the Protein Society, 15(5), 1042-50. https://doi.org/10.1110/ps.062115406

The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. / Nardini, Marco; Svergun, Dmitri; Konarev, Peter V; Spanò, Stefania; Fasano, Mauro; Bracco, Chiara; Pesce, Alessandra; Donadini, Alessandra; Cericola, Claudia; Secundo, Francesco; Luini, Alberto; Corda, Daniela; Bolognesi, Martino.

In: Protein science : a publication of the Protein Society, Vol. 15, No. 5, 05.2006, p. 1042-50.

Research output: Contribution to journalArticle

Nardini, M, Svergun, D, Konarev, PV, Spanò, S, Fasano, M, Bracco, C, Pesce, A, Donadini, A, Cericola, C, Secundo, F, Luini, A, Corda, D & Bolognesi, M 2006, 'The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured', Protein science : a publication of the Protein Society, vol. 15, no. 5, pp. 1042-50. https://doi.org/10.1110/ps.062115406
Nardini, Marco ; Svergun, Dmitri ; Konarev, Peter V ; Spanò, Stefania ; Fasano, Mauro ; Bracco, Chiara ; Pesce, Alessandra ; Donadini, Alessandra ; Cericola, Claudia ; Secundo, Francesco ; Luini, Alberto ; Corda, Daniela ; Bolognesi, Martino. / The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. In: Protein science : a publication of the Protein Society. 2006 ; Vol. 15, No. 5. pp. 1042-50.
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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.",
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AB - 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.

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