Relevant references for this domain

Primary literature for the DIM1 domain is listed below.

Identification, characterization and crystal structure analysis of the humanspliceosomal U5 snRNP-specific 15 kD protein.

Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R
J Mol Biol. 1999; 294: 515-25

The U5 small ribonucleoprotein particle (snRNP) contains various proteinsinvolved in catalytic activities mediating conformational rearrangements of thespliceosome. We have isolated and characterized the evolutionarily highlyconserved human U5 snRNP-specific protein U5-15kD. The crystal structure ofU5-15kD determined at 1.4 A resolution revealed a thioredoxin-like fold andrepresents the first structure of a U5 snRNP-specific protein known so far. With respect to human thioredoxin the U5-15kD protein contains 37 additional residues causing structural changes which most likely form putative binding sites forother spliceosomal proteins or RNA. Moreover, a novel intramolecular disulfidebond replaces the canonical one found in the thioredoxin family. Even thoughU5-15kD appears to lack protein disulfide isomerase activity, it is strictlyrequired for pre-mRNA splicing in vivo as we demonstrate by genetic depletion of its ortholog in Saccharomyces cerevisiae. Our data suggest that the previouslyreported involvement of its Schizosaccharomyces pombe ortholog Dim1p in cellcycle regulation is a consequence of its essential role in pre-mRNA splicing.