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PROSITE documentation PDOC50304

Tudor domain profile





Description

The Tudor domain is a domain of around 50-70 amino acids which was first identified as a repeat present in 10 copies in Drosophila Tudor protein [1,2]. The Tudor domain is found in one or several copies in many eukaryotic proteins that colocalize with ribonucleoprotein or single-stranded DNA-associated complexes in the nucleus, in the mitochondrial membrane, or at kinetochores. The Tudor domain can be found in association with other domains, such as a staphylococcal nuclease (SN)-fold (see <PDOC00865>), a OTU domain (see <PDOC50802>), a KH domain (see <PDOC50084>), a DEAD/DEAH box helicase domain (see <PDOC00039>) or a coiled-coil domain. An insufficient amount of functional information concerning the proteins containing a Tudor domain is currently available from which to ascribe putative functions to Tudor domains. However, it is likely that Tudor domains function as protein-protein interaction motifs during RNA metabolism and/or transport and do not bind to RNA directly [1,3,4].

The resolution of the solution structure of the Tudor domain of human SMN revealed that the Tudor domain forms a strongly bent antiparallel β-sheet with five strands forming a barrel-like fold. The structure exhibits a conserved negatively charged surface that interacts with the C-terminal Arg and Gly-rich tails of the spliceosomal Sm D1 and D3 proteins [4].

Some proteins known to contain a Tudor domain are listed below:

  • Drosophila Tudor, a protein required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation.
  • Drosophila Homeless (HLS), a protein belonging to the DE-H family of RNA- dependent ATPases that is required for RNA localization during oogenesis. HLS might function during the processing of pre-mRNA whose products direct microtubules organization, which is required for mRNA transport.
  • Drosophila ovarian tumor protein (OTU). OTU is required at multiple stages of oogenesis and the Tudor domain is required for its early function. A portion of OTU cofractionates with mRNA/protein complexes (mRNPs) [5].
  • Mammalian survival of motor neuron protein (SMN). SMN participates in small nuclear ribonucleoprotein (snRNP) particles assembly in the cytoplasm and may also affect splicing more directly in the nucleus. In human, defects of the SMN protein are associated with spinal muscular atrophy (SMA), a disease in which the anterior horn cells in the spinal corn die, resulting in progressive muscle weakness and ultimately, in some cases, in the inability to breathe and swallow.
  • Human A-kinase anchor protein 1 (AKAP1). It binds to type I and II regulatory subunits of protein kinase a and anchors them to the cytoplasmic face of the mitochondrial outer membrane. An alternatively spliced version of AKAP1 (S-AKAP84) participates in spermiogenesis, probably by facilitating ordering of spermatid mitochondria.
  • Human p100, a nuclear protein that coactivates gene expression mediated by the Epstein-Barr virus nuclear antigen 2 (EBNA-2). The p100 protein is also able to bind single-stranded DNA.
  • Human Tudor and KH domain-containing protein (TDRKH) [6].
  • Rat Tudor repeat associator with PCTAIRE 2 (Trap). Trap contains five Tudor domains and interacts with the N-terminal domain of PCTAIRE 1 and 2, members of Cdk-related kinases which is highly expressed in the nervous system.
  • Caenorhabditis elegans hypothetical protein C56G2.1.
  • Rice Rp120, a protein that binds to a wide range of mRNAs expressed during seed development and is associated with the cytoskeleton [7].

The profile we developed covers the entire Tudor domain.

Last update:

December 2001 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

TUDOR, PS50304; Tudor domain profile  (MATRIX)


References

1AuthorsPonting C.P.
TitleTudor domains in proteins that interact with RNA.
SourceTrends Biochem. Sci. 22:51-52(1997).
PubMed ID9048482

2AuthorsCallebaut I. Mornon J.-P.
TitleThe human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development.
SourceBiochem. J. 321:125-132(1997).
PubMed ID9003410

3AuthorsHirose T. Kawabuchi M. Tamaru T. Okumura N. Nagai K. Okada M.
TitleIdentification of tudor repeat associator with PCTAIRE 2 (Trap). A novel protein that interacts with the N-terminal domain of PCTAIRE 2 in rat brain.
SourceEur. J. Biochem. 267:2113-2121(2000).
PubMed ID10727952

4AuthorsSelenko P. Sprangers R. Stier G. Buehler D. Fischer U. Sattler M.
TitleSMN tudor domain structure and its interaction with the Sm proteins.
SourceNat. Struct. Biol. 8:27-31(2001).
PubMed ID11135666
DOI10.1038/83014

5AuthorsGlenn L.E. Searles L.L.
TitleDistinct domains mediate the early and late functions of the Drosophila ovarian tumor proteins.
SourceMech. Dev. 102:181-191(2001).
PubMed ID11287191

6AuthorsLamb F.S. Barna T.J. Goud C. Marenholz I. Mischke D. Schutte B.C.
TitleComplex RNA processing of TDRKH, a novel gene encoding the putative RNA-binding tudor and KH domains.
SourceGene 246:209-218(2000).
PubMed ID10767542

7AuthorsSami-Subbu R. Choi S.-B. Wu Y. Wang C. Okita T.W.
SourcePlant Mol. Biol. 46:79-88(2001).



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