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. 1991 Oct 18;67(2):335-42.
doi: 10.1016/0092-8674(91)90185-2.

Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing

H Li  1 , P M Bingham
Affiliations

Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing

H Li et al. Cell. .

Abstract

Two unrelated pre-mRNA splicing regulators-suppressor-of-white-apricot (su(wa)) and transformer (tra)-contain distinctive, approximately 120 amino acid arginine/serine (RS)-rich domains. Deletion of the su(wa) RS domain eliminates function. Replacement with the tra RS domain restores su(wa) function to nearly wild-type levels. Replacement with a 10 amino acid simple nuclear entry signal allows partial, inefficient function. Thus, the su(wa) RS domain apparently serves a generic function(s) subsuming nuclear entry. Moreover, immunocytochemical studies demonstrate that both RS domains specifically direct localization of a fused reporter protein to a punctate subnuclear compartment shown previously to be enriched in several constitutive splicing components. We propose that RS domains are a new class of targeting signals directing concentration of proteins in a subnuclear compartment implicated in splicing metabolism.

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