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Janowski, R. ; Niessing, D.

The large family of PC4-like domains - similar folds and functions throughout all kingdoms of life.

RNA Biol. 17, 1228-1238 (2020)
Verlagsversion Forschungsdaten DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
RNA- and DNA-binding domains are essential building blocks for specific regulation of gene expression. While a number of canonical nucleic acid binding domains share sequence and structural conservation, others are less obviously linked by evolutionary traits. In this review, we describe a protein fold of about 150 aa in length, bearing a conserved beta-beta-beta-beta-alpha-linker-beta-beta-beta-beta-alpha topology and similar nucleic acid binding properties but no apparent sequence conservation. The same overall fold can also be achieved by dimerization of two proteins, each bearing a beta-beta-beta-beta-alpha topology. These proteins include but are not limited to the transcription factors PC4 and P24 from humans and plants, respectively, the human RNA-transport factor Pur-alpha (also termed PURA), as well as the ssDNA-binding SP_0782 protein fromStreptococcus pneumoniaand the bacteriophage coat proteins PP7 and MS2. Besides their common overall topology, these proteins share common nucleic acids binding surfaces and thus functional similarity. We conclude that these PC4-like domains include proteins from all kingdoms of life and are much more abundant than previously known.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Rna ; Dna Binding ; Pc4-like ; Protein Domain ; Protein Fold ; Structural Biology ; Topology ; Pura ; Rrm ; Kh-domain; Single-stranded-dna; Rna-binding Proteins; C-terminal Domain; Pur-alpha; Trypanosoma-brucei; Crystal-structure; Molecular-basis; Guide-rna; Transcription Factors; Structural Basis
Sprache englisch
Veröffentlichungsjahr 2020
HGF-Berichtsjahr 2020
ISSN (print) / ISBN 1547-6286
e-ISSN 1555-8584
Zeitschrift RNA Biology
Quellenangaben Band: 17, Heft: 9, Seiten: 1228-1238 Artikelnummer: , Supplement: ,
Verlag Landes Bioscience
Verlagsort 530 Walnut Street, Ste 850, Philadelphia, Pa 19106 Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503091-001
DOI 10.1080/15476286.2020.1761639
WOS ID WOS:000544224400001
Scopus ID 85086658561
PubMed ID 32476604
Erfassungsdatum 2020-06-03
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