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Peer-reviewedCC BY 4.0PLOS One

The G-patch protein Cwf28 interacts with the RNA helicase Cdc28 in catalytically active spliceosomes in Schizosaccharomyces pombe

  • Laura Olivia Karika1
  • Ingrid Cipakova2
  • Miroslava Kretova3
  • Tomas Selicky
  • Natalia Cmikova
  • Daniela Nemcekova
  • Lenka Kohutova
  • Peter Barath
  • Lubos Cipak
  1. 1Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Bratislava, Slovakia
  2. 2Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden
  3. 3Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia
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Abstract

G-patch proteins are emerging as key regulatory cofactors of DEAH-box RNA helicases involved in pre-mRNA splicing, yet the functions of many family members remain poorly understood. Here, we characterize the conserved G-patch domain–containing protein Cwf28 from Schizosaccharomyces pombe, an essential factor with a previously unclear molecular function, and define its role within the spliceosome. Tandem affinity purification coupled with mass spectrometry revealed that Cwf28 predominantly associates with components of the Prp19 complex (NTC) and factors involved in the catalytic activation and progression of the spliceosome, placing it within catalytically active spliceosomal assemblies. Gene ontology analysis showed enrichment of the Cwf28 interactome in factors involved in spliceosome assembly, activation, and catalytic remodeling. Notably, the DEAH-box RNA helicase Cdc28, the ortholog of human DHX16 and Saccharomyces cerevisiae Prp2, was identified as the most abundant interactor. Further analysis demonstrated that Cwf28 interacts with Cdc28 via its conserved G-patch domain, and domain mapping confirmed that this interaction is G-patch domain dependent. Together, these findings identify Cwf28 as a component of catalytically active spliceosomes and suggest a potential role for Cwf28 in modulating the activity of the RNA helicase Cdc28, providing insight into conserved mechanisms underlying RNA helicase regulation during splicing.

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Cite

BibTeXRIS
BibTeX
@article{karika2026gpatch,
  title = {{The G-patch protein Cwf28 interacts with the RNA helicase Cdc28 in catalytically active spliceosomes in Schizosaccharomyces pombe}},
  author = {Laura Olivia Karika and Ingrid Cipakova and Miroslava Kretova and Tomas Selicky and Natalia Cmikova and Daniela Nemcekova and Lenka Kohutova and Peter Barath and Lubos Cipak},
  journal = {PLOS One},
  year = {2026},
  month = sep,
  doi = {10.1371/journal.pone.0357276},
  url = {https://doi.org/10.1371/journal.pone.0357276},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - The G-patch protein Cwf28 interacts with the RNA helicase Cdc28 in catalytically active spliceosomes in Schizosaccharomyces pombe
AU  - Laura Olivia Karika
AU  - Ingrid Cipakova
AU  - Miroslava Kretova
AU  - Tomas Selicky
AU  - Natalia Cmikova
AU  - Daniela Nemcekova
AU  - Lenka Kohutova
AU  - Peter Barath
AU  - Lubos Cipak
PY  - 2026
DA  - 2026/09/03
JO  - PLOS One
DO  - 10.1371/journal.pone.0357276
UR  - https://doi.org/10.1371/journal.pone.0357276
AB  - G-patch proteins are emerging as key regulatory cofactors of DEAH-box RNA helicases involved in pre-mRNA splicing, yet the functions of many family members remain poorly understood. Here, we characterize the conserved G-patch domain–containing protein Cwf28 from Schizosaccharomyces pombe, an essential factor with a previously unclear molecular function, and define its role within the spliceosome. Tandem affinity purification coupled with mass spectrometry revealed that Cwf28 predominantly associates with components of the Prp19 complex (NTC) and factors involved in the catalytic activation and progression of the spliceosome, placing it within catalytically active spliceosomal assemblies. Gene ontology analysis showed enrichment of the Cwf28 interactome in factors involved in spliceosome assembly, activation, and catalytic remodeling. Notably, the DEAH-box RNA helicase Cdc28, the ortholog of human DHX16 and Saccharomyces cerevisiae Prp2, was identified as the most abundant interactor. Further analysis demonstrated that Cwf28 interacts with Cdc28 via its conserved G-patch domain, and domain mapping confirmed that this interaction is G-patch domain dependent. Together, these findings identify Cwf28 as a component of catalytically active spliceosomes and suggest a potential role for Cwf28 in modulating the activity of the RNA helicase Cdc28, providing insight into conserved mechanisms underlying RNA helicase regulation during splicing.
SN  - 1932-6203
ER  -