PROSITE documentation PDOC51879
RST domain profiles


The RST (for RCD1 SRO TAF4) domain is a plant-specific domain found in WWE-PARPs (poly(ADP-ribose) polymerase) (see <PDOC50918> and <PDOC51059>) and TAF4s (TBP-Associated Factor 4), a component of several multimeric protein complexes including primarily the general transcription factor TFIID involved in transcriptional initiation. The RST domain is a protein-protein interaction domain suggested to be critical for the interaction with several, mostly plant-specific transcription factors [1,2].

The RST domain structure has a unique helical arrangement composed of four α helices flanked by disordered termini (see <PDB:5OAO>). The four-helix fold of the RST domain organizes in an open, hydrophobic L-shape with room for catching the ligand [3]. A strong conservation of a large number of aliphatic amino acids in the N- and C-termini of the RST domain, with a conserved tyrosine in the middle of the domain and two conserved positively charged amino acids in the second half of the domain, is striking [1].

The profile we developed covers the entire RST domain.

Last update:

November 2018 / First entry.


Technical section

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

RST, PS51879; RST domain profile  (MATRIX)


1AuthorsJaspers P. Overmyer K. Wrzaczek M. Vainonen J.P. Blomster T. Salojaervi J. Reddy R.A. Kangasjaervi J.
TitleThe RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants.
SourceBMC Genomics 11:170-170(2010).
PubMed ID20226034

2AuthorsJaspers P. Blomster T. Brosche M. Salojaervi J. Ahlfors R. Vainonen J.P. Reddy R.A. Immink R. Angenent G. Turck F. Overmyer K. Kangasjaervi J.
TitleUnequally redundant RCD1 and SRO1 mediate stress and developmental responses and interact with transcription factors.
SourcePlant J. 60:268-279(2009).
PubMed ID19548978

3AuthorsBugge K. Staby L. Kemplen K.R. O'Shea C. Bendsen S.K. Jensen M.K. Olsen J.G. Skriver K. Kragelund B.B.
TitleStructure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alphaalpha-Scaffold for Disorder in Transcriptional Networks.
SourceStructure 26:734-746.e7(2018).
PubMed ID29657132

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