RESUMEN
Here, we demonstrated the involvement of the domains in Arabidopsis high-light responsive serine/arginine-rich (SR) and SR-like proteins, atSR30 and atSR45a, respectively, in subcellular and subnuclear distribution using a series of structural domain-deleted mutants. Judging from the localization of the transiently expressed domain-deleted mutants in onion epidermal cells, the C terminal low complexity domain rich in arginine-serine repeats (C-RS) domain of atSR30 appeared to be necessary for the nuclear localization. On the other hand, the N-terminal RS (N-RS) domain of atSR45a was necessary for the accurate nuclear localization, although the N- or C-RS domain alone was sufficient for the nuclear speckled organization. The phosphorylation of RS domains of atSR45a is irrelevant to the regulation of its localization. atSR45a and atSR30 were co-localized in the speckles, suggesting their collaborative roles in the regulation of alternative splicing events.