Cyril Dominguez


Tel: +44 (0)116 229 7073

Personal details

  • BSc in Biochemistry, University of Aix-Marseille II, France, 1998
  • DEA (MSc) in Nutritional Biochemistry, University of Aix-Marseille III, Marseille, France, 1999
  • PhD: NMR Department, University of Utrecht, Utrecht, The Netherlands, 2000-2004
  • Postdoctoral Fellow, Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland, 2004-2010
  • Joined Department of Biochemistry as a Lecturer and MRC Fellow in 2010


25- Danilenko M., Dalgliesh C., Pagliarini V., Naro C., Ehrmann I., Feracci M., Kheirollahi-Chadegani M., Tyson-Capper A., Clowry G.J., Fort P., Dominguez C., Sette C., Elliott D.J. (2017).
Binding site density enables paralog-specific activity of SLM2 and Sam68 proteins in Neurexin2 AS4 splicing control.
Nucleic Acids Res., advance online publication
24- Weldon C., Eperon I.C., Dominguez C. (2016).
Do we know whether G-quadruplexes actually form in long functional RNA molecules?
Biochem Soc Trans, 44, 1761-68
23- Weldon C., Behn-Ansmant I., Burley G.A., Hurley L.H., Branlant C., Eperon I.C., and Dominguez C. (2016).
Identification of G-quadruplexes using 7-deaza-guanine substituted RNA.
Nat. Chem. Biol., 13, 18-20
22- Feracci M., Foot J.N., Grellscheid S.N., Danilenko M., Stehle R., Gonchar O., Kang H.S., Meyer N.H., Liu Y., Lahat A., Sattler M., Eperon I.C., Elliott D.J., and Dominguez C. (2016).
Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.
Nat. Comms, 7, 10355
21- Feracci M., Foot J.N., and Dominguez C. (2014).
Structural investigations of the RNA-binding properties of STAR proteins.
Biochem. Soc. Trans., 42(4), 1141-6
20- Foot J.N.*, Feracci M.*, and Dominguez C. (2014).
Screening protein – single stranded RNA complexes by NMR spectroscopy for structure determination.
Methods, 65, 288-301.
19- Theler D., Dominguez C., Blatter M., Boudet J., and Allain F.H-T (2014).
Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA.
Nucleic Acids Res., 42, 13911-9
18- Back R., Dominguez C., Rothé B., Bobo C., Beaufils C., Moréra S., Meyer P., Charpentier P., Branlant C., Allain F.H.-T., and Manival X. (2013).
NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explains how Hsp90 recognizes the R2TP complex.
Structure, 21, 1834-47.
17- Samatanga B., Dominguez C., Jelezarov I., Allain F.H-.T. (2013)
The high kinetic stability of a G-quadruplex limits hnRNP F qRRM3 binding to G-tract RNA
Nucleic Acids Res., 41, 2505-16
16- Schubert M., Dominguez C., Duss O., Ravindranathan S. and Allain F.H.-T (2011)
Structure determination and dynamics of protein-RNA complexes using NMR spectroscopy
Advances in Biomedical Spectroscopy, Volume 3, 249-278.
Abstract + Full text
15- Cléry A., Jayne S., Benderska N., Dominguez C. , Stamm S. and Allain F.H.-T. (2011)
Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1
Nat. Struct. Mol. Biol., 18, 443-50.
Abstract, Full text
14- Dominguez C.*, Schubert M.*, Duss O.*, Ravindranathan S.* and Allain F.H.-T* (2011)
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy
Prog. Nuc. Mag. Res. Spec., 58, 1-61.
Abstract, Full text
13- Dominguez C., Fisette J.F., Chabot B., Allain F.H.-T. (2010).
Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs
Nat. Struct. Mol. Biol., 17, 853-61
Abstract, Full Text
12- Dominguez C. and Allain F.H.-T. (2006)
NMR structure of the three quasi RNA Recognition Motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: A novel mode of RNA recognition
Nucleic Acids Res., 34, 3634-3645
Abstract, Full text
11- Dominguez C., and Allain F.H.-T. (2005)
Resonance assignments of the N-terminal RNA recognition motifs (RRM) of the human heterogeneous nuclear ribonucleoprotein F (HnRNP F)
J. Biomol. NMR, 33, 282
Abstract, Full text
10- Maris C.*, Dominguez C.* and Allain F.H.-T. (2005)
The RNA recognition motif, a plastic RNA binding platform to regulate posttranscriptional gene expression
FEBS Journal, 272, 2118-2131
Abstract, Full text
9- van Dijk A.D.J., de Vries S.J., Dominguez C., Chen H., Zhou H.X. and Bonvin A.M.J.J. (2005)
Data-driven docking: HADDOCK’s adventures in CAPRI
Proteins, 60, 232-238
Abstract, Full text
8- Houben K., Wasielewski E., Dominguez C., Kellenberger E., Atkinson R.A., Timmers H.Th.M., Kieffer B. and Boelens R. (2005)
Dynamics and metal exchange properties of C4C4 RING domains from CNOT4 and the p44 subunit of TFIIH
J. Mol. Biol., 349(3), 621-637
Abstract, Full text
7- Kellenberger E., Dominguez C., Fribourg S., Wasielewski E., Moras D., Poterszman A., Boelens R. and Kieffer B. (2005)
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions
J. Biol. Chem., 280(21), 20785-20792
Abstract, Full text
6- Houben K.*, Dominguez C.*, van Schaik F.M.A., Timmers H.Th.M., Bonvin A.M.J.J. and Boelens R. (2004)
Solution structure of the Ubiquitin-conjugating enzyme UbcH5B
J. Mol. Biol., 344(2), 513-526
Abstract, Full text
5- Dominguez C., Bonvin A.M.J.J., Winkler G.S., van Schaik F.M.A., Timmers H.Th.M. and Boelens R. (2004)
Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis and docking approaches
Structure, 12(4), 633-644
Abstract, Full text
4- Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I.A., Boelens R. and Timmers H.Th.M. (2004)
An altered-specificity Ubiquitin-conjugating enzyme/Ubiquitin-protein ligase pair
J. Mol. Biol., 337(1), 157-165
Abstract, Full text
3- Dominguez C., Folkers G.E. and Boelens R. (2003)
RING Domain Proteins
Contribution to "Handbook of metalloproteins", Volume 3, John Wiley and Son, 338-351
2- Dominguez C., Boelens R. and Bonvin A.M.J.J. (2003)
HADDOCK: A Protein-Protein Docking Approach Based on Biochemical or Biophysical Information
J. Am. Chem. Soc., 125(7) pp. 1731 - 1737
Abstract, Full text
Go to the HADDOCK webpage
1- Dominguez C., Sebban-Kreuzer C., Bornet O., Kerfelec B., Chapus C. and Guerlesquin F. (2000)
Interactions of bile salt micelles and colipase studied through intermolecular nOes
FEBS Letters, 482 (1-2), pp. 109-112
Abstract, Full text

*: equal contribution

Other publications:

Dominguez C. (2004)
NMR-based docking of protein-protein complexes: the human UbcH5B-CNOT4 ubiquitination complex
Ph.D Thesis, Utrecht University
ISBN: 90-393-3721-7
Abstract + Full text


  • Structural Biology (NMR Spectroscopy, Docking)
  • Post-transcriptional gene regulation, alternative pre-mRNA splicing
  • Structural studies of macromolecular complexes


Molecular mechanisms connecting signal transduction and pre-mRNA alternative splicing

Cellular processes are tightly regulated at different levels by various signaling pathways depending on extracellular stimulations. Extensive research over many years has identified numerous signaling pathways that influence the regulation of gene transcription and hence, it was thought, the fundamental properties of the cell.

More recently, it has been demonstrated that post-transcriptional gene regulation
is at least, and even possibly more, important than transcription regulation. However,
the main pathways governing regulation remain to be elucidated. For many years,
RNA molecules, especially messenger RNAs (mRNAs) were considered as passive
molecules. It is now clear that numerous RNA binding proteins play an important role
in many cellular functions. These proteins regulate gene expression at different levels. The main post-transcriptional gene regulation events include alternative splicing, RNA export and stability and translation of mRNAs.

Alternative splicing

In eukaryotes, gene transcription produces a pre-messenger RNA (pre-mRNA) that
contains alternating sequences, the introns and the exons. Constitutive splicing
consists of removing the introns from the pre-mRNA and joining the exons producing a mature mRNA. This event is catalyzed by a large macromolecular complex, the
spliceosome, that specifically recognizes splice sites, the conserved nucleotide
sequences that comprise exon/intron junctions. However, splicing can lead to many
different mRNAs from a single pre-mRNA. This process is called alternative splicing.
Alternative splicing describes the regulated process of differential inclusion or
exclusion of certain regions of the pre-mRNA. This process allows the production, from a single gene, of many protein isoforms that can have different cellular functions. Alternative splicing is thus an important source of protein diversity from a limited number of genes. Recently, it was shown that more than 90% of the protein-coding genes in the human genome undergo alternative splicing.

Alternative splicing

Alternative splicing is possible because eukaryotic pre-mRNAs possess multiple potential splice sites. Some are located at the exon/intron junctions and are used during constitutive splicing. Many others are located in exons and introns and are recognized by the spliceosome only under certain conditions. The use of a splice site depends on the recognition of the pre-mRNA by specific RNA binding proteins, the splicing factors. These proteins recognize specifically short RNA sequences, the cis-acting elements, which are generally located near splice sites. The binding of splicing factors to these cis-acting elements affects the use of nearby splice sites.

Current views suggest that numerous splicing factors may compete to enhance or
inhibit the use of a specific splice site. Alternative splicing regulation is therefore often modulated by the relative concentrations of these splicing factors in the nucleus. This modulation is achieved by different manners: some splicing factors may be expressed only at certain stages of the development or only in specific tissues. Alternatively, the nuclear localization of these splicing factors can be regulated by post-translational modifications, such as phosphorylation, that affect the distribution of these factors between the nucleus and the cytoplasm. As a consequence, many specific protein isoforms are produced by alternative splicing either in certain developmental stages or tissues, or as a consequence of regulation by extracellular signaling mechanisms.

The relationship between signaling pathways and post-transcriptional gene regulation, however, is still poorly understood.

Research interests

Our main research interest is therefore to understand at the molecular level the interplay between signaling pathways and post-transcriptional gene regulation. To this aim, we are studying protein-protein and protein-RNA complexes using structural biology techniques (NMR and X-ray) and biophysical methods (isothermal titration calorimetry, ITC).

In addition, our structural work is complemented by functional assays thank to collaboration with the group of Professor Ian Eperon within the department of Molecular and Cellular Biology.

You can also view our research highlights online.

Group members

Postdoctoral Fellows:

PhD students:

A PhD position is available in our laboratory starting in October 2017

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Contact Details

Department of Molecular and Cell Biology
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F:  +44(0)116 229 7123


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Redfearn Lecture 2017

To Be Confirmed