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

doi:10.1110/ps.062115406

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

Medical Sciences

Research output: Contribution to journal › Article › peer-review

39 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 language	English
Pages (from-to)	1042-50
Number of pages	9
Journal	Protein science : a publication of the Protein Society
Volume	15
Issue number	5
DOIs	https://doi.org/10.1110/ps.062115406
Publication status	Published - 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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Nardini, M., Svergun, D., Konarev, P. V., 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, 15(5), 1042-50. https://doi.org/10.1110/ps.062115406

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

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title = "The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured",

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.",

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",

author = "Marco Nardini and Dmitri Svergun and Konarev, {Peter V} and Stefania Span{\`o} and Mauro Fasano and Chiara Bracco and Alessandra Pesce and Alessandra Donadini and Claudia Cericola and Francesco Secundo and Alberto Luini and Daniela Corda and Martino Bolognesi",

year = "2006",

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doi = "10.1110/ps.062115406",

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T1 - The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured

AU - Nardini, Marco

AU - Svergun, Dmitri

AU - Konarev, Peter V

AU - Spanò, Stefania

AU - Fasano, Mauro

AU - Bracco, Chiara

AU - Pesce, Alessandra

AU - Donadini, Alessandra

AU - Cericola, Claudia

AU - Secundo, Francesco

AU - Luini, Alberto

AU - Corda, Daniela

AU - Bolognesi, Martino

PY - 2006/5

Y1 - 2006/5

N2 - 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.

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.

KW - Alcohol Oxidoreductases

KW - Amino Acid Sequence

KW - Binding Sites

KW - Circular Dichroism

KW - DNA-Binding Proteins

KW - Magnetic Resonance Spectroscopy

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Phosphoproteins

KW - Protein Folding

KW - Repressor Proteins

KW - Transcription Factors

KW - Transcription, Genetic

U2 - 10.1110/ps.062115406

DO - 10.1110/ps.062115406

M3 - Article

C2 - 16597837

SN - 0961-8368

VL - 15

SP - 1042

EP - 1050

JO - Protein science : a publication of the Protein Society

JF - Protein science : a publication of the Protein Society

IS - 5

ER -

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

Abstract

Keywords

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