PUA domain

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PUA domain
PDB 2cx1 EBI.jpg
Cartoon representation of the molecular structure of the crystal structure of the PUA domain-containing protein APE0525 from Aeropyrum pernix HB8 ( PDB: 2cx1 ​)
Identifiers
SymbolPUA
Pfam clan CL0178
ECOD 1.1.9

In molecular biology, the PUA domain (Pseudouridine synthase and Archaeosine transglycosylase domain) is an ancient RNA-binding domain. [1]

Contents

Structure

The PUA domain consists of 64-96 amino acids forming a compact alpha/beta fold. It shows six beta-strands and two alpha-helices that cap the structure. [2]

Function

The PUA domain is found in diverse protein families [1] involved in:

RNA recognition mechanism

The PUA domain uses a distinctive "double-edged ledge" formed by the alpha1-beta2 loop and beta6 strand for RNA binding while an "adjacent cleft" alpha1-beta2 accommodates single-stranded RNA overhangs. It has two main binding modes: the sideways binding recognizes minor groove of double-stranded RNA stems; and the terminal binding recognizes the bottom/terminal end of RNA stems across the major groove. [1]

Evolution and distribution

Proteins with the PUA domain are found across bacteria, archaea, and eukaryotes. This domain has evolved as a flexible RNA interaction module, with different proteins using variations in amino acid composition to achieve specific RNA recognition patterns while maintaining the core structural framework. [1]

Clinical Relevance

PUA domain proteins are essential for fundamental cellular processes. [2] Some examples of associated diseases are:

References

  1. 1 2 3 4 Pérez-Arellano, Isabel; Gallego, José; Cervera, Javier (2007). "The PUA domain - a structural and functional overview". The FEBS Journal. 274 (19): 4972–4984. doi:10.1111/j.1742-4658.2007.06031.x. ISSN   1742-464X. PMID   17803682.
  2. 1 2 Cerrudo, Carolina S.; Ghiringhelli, Pablo D.; Gomez, Daniel E. (2014). "Protein universe containing a PUA RNA-binding domain". The FEBS Journal. 281 (1): 74–87. doi:10.1111/febs.12602. hdl: 11336/32610 . ISSN   1742-4658. PMID   24393395.
  3. ↑ Garus, Alexandre; Autexier, Chantal (2021). "Dyskerin: an essential pseudouridine synthase with multifaceted roles in ribosome biogenesis, splicing, and telomere maintenance". RNA. 27 (12): 1441–1458. doi:10.1261/rna.078953.121. ISSN   1469-9001. PMC   8594475 . PMID   34556550.
  4. ↑ Silva, Ana; Cerqueira, Mónica Costa; Rosa, Beatriz; Sobral, Catarina; Pinto-Ribeiro, Filipa; Costa, Marta Freitas; Baltazar, Fátima; Afonso, Julieta (2023-03-07). "Prognostic Value of Monocarboxylate Transporter 1 Overexpression in Cancer: A Systematic Review". International Journal of Molecular Sciences. 24 (6): 5141. doi: 10.3390/ijms24065141 . ISSN   1422-0067. PMC   10049181 . PMID   36982217.
  5. ↑ Mattioli, Francesca; Worpenberg, Lina; Li, Cai-Tao; Ibrahim, Nazia; Naz, Shagufta; Sharif, Saima; Firouzabadi, Saghar G.; Vosoogh, Shohreh; Saraeva-Lamri, Radoslava; Raymond, Laure; Trujillo, Carlos; Guex, Nicolas; Antonarakis, Stylianos E.; Ansar, Muhammad; Darvish, Hossein (2023). "Biallelic variants in NSUN6 cause an autosomal recessive neurodevelopmental disorder". Genetics in Medicine. 25 (9): 100900. doi:10.1016/j.gim.2023.100900. ISSN   1530-0366. PMID   37226891.
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