Inclusion of Hsp70 co-chaperone and RNA binding activities facilitate optimal function of spliceosomal disassembly factor Cwf23 in intron-rich Schizosaccharomyces pombe

Cwc23 is an essential J-domain protein that collaborates with the disassembly factor Ntr1 to facilitate spliceosomal disassembly. Although Cwc23 orthologs have been identified in spliceosomal extracts of many eukaryotes, their functionality in intron-rich eukaryotes remains largely unexplored. Here, we investigate the functionality of Cwf23, an ortholog of Cwc23 in Schizosaccharomyces pombe . Our study reveals that while the interaction between Cwf23 and Sp Ntr1 is conserved, it is not essential in S. pombe . Additionally, the RNA recognition motif (RRM) in Cwf23 is crucial for its function, as mutations in the RRM affect both growth and pre-mRNA splicing. Unlike its budding yeast counterpart, the J-domain of Cwf23 is indispensable, as J-domain mutants cannot support cell viability. These findings suggest a new paradigm in which the presence of a functional RRM and the essential nature of the J-domain underscore the increased requirements for an RNA-binding Hsp70 co-chaperone machinery in spliceosomal remodelling in “intron-rich” eukaryotes.