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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC52058
Zinc finger UVSSA-type profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC52058

Description

Transcription is an essential cellular process in which RNA polymerase II (RNAPII) synthesizes complementary copies of protein-coding and non-coding genes. Lesions on the template DNA strand cause stalling of elongating RNAPII and trigger a genome-wide transcriptional arrest. Transcription-coupled repair (TCR) is a dedicated pathway for the preferential repair of bulky transcription-blocking DNA lesions. These lesions stall the elongating RNAPII triggering the recruitment of TCR proteins at the damaged site. UV-stimulated scaffold protein A (UVSSA) is a cofactor which is involved in stabilization of the TCR complex, recruitment of DNA-repair machinery and removal/restoration of RNAPII from the lesion site.

UVSSA homologs are present across the eukaryotic kingdoms including unicellular eukaryotes like Dictyostelium. In metazoans, the protein is observed in primitive metazoans like Hydra vulgaris and C. elegans to non-vertebrates and vertebrate species. Surprisingly, the UVSSA homologs are missing in a few insect species including Drosophila. In plants, UVSSA homologs are present in algae species like Chlamydomonas to early vascular system plants like Selaginella to higher order land plants. In fungal genomes, it is present in Zygomycota and Chytridiomycota divisions of fungi, including common bread mould Mucor and Rhizopus. However, it is not observed in Ascomycota and Basidiomycota divisions of fungi [1,2].

UVSSA contains a zinc (Zn)-finger that docks on the RNAPII jaw: both knuckles of the finger insert their residues into a shallow groove formed by helix 1, consecutive β-strand and helix 3 of the jaw domain [2].

The profile we developed covers the entire UVSSA-type zinc finger.

Last update:

February 2025 / First entry.

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Technical section

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

ZF_UVSSA, PS52058; Zinc finger UVSSA-type profile  (MATRIX)


References

1AuthorsMistry H. Gupta G.D.
TitleTranscription coupled DNA repair protein UVSSA binds to DNA and RNA: Mapping of nucleic acid interaction sites on human UVSSA.
SourceArch. Biochem. Biophys. 735:109515-109515(2023).
PubMed ID36623745
DOI10.1016/j.abb.2023.109515

2AuthorsKokic G. Yakoub G. van den Heuvel D. Wondergem A.P. van der Meer P.J. van der Weegen Y. Chernev A. Fianu I. Fokkens T.J. Lorenz S. Urlaub H. Cramer P. Luijsterburg M.S.
TitleStructural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair.
SourceNat. Struct. Mol. Biol. 31:536-547(2024).
PubMed ID38316879
DOI10.1038/s41594-023-01207-0



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