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Vol. 13, No. 12, pp. 1513-1518, June 15, 1999

RESEARCH COMMUNICATION
Developmental regulation of SR protein phosphorylation and activity

Jeremy R. Sanford, and James P. Bruzik1

Center for RNA Molecular Biology, Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106 USA

Serine/arginine-rich splicing factors (SR proteins) are substrates for serine phosphorylation that can regulate SR protein function. We have observed gross changes in SR protein phosphorylation during early development coincident with major zygotic gene activation in the nematode Ascaris lumbricoides. These differences correlate with large-scale changes in SR protein activity in promoting both trans- and cis-splicing. Importantly, inactive early stage extracts can be made splicing competent on addition of later stage SR proteins. These data suggest that changes in SR protein phosphorylation have a role in the activation of pre-mRNA splicing during early development.

[Key Words: SR protein; splicing factor; phosphorylation; development]


GENES & DEVELOPMENT 13:1513-1518 © 1999 by Cold Spring Harbor Laboratory Press  ISSN 0890-9369/99 $5.00

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