Nucleic Acids Research, Vol 27, Issue 13 2618-2626, Copyright © 1999 by Oxford University Press
M Lutzelberger, T Gross and NF Kaufer
We isolated srp2, a gene encoding a protein composed of two RNA binding
domains (RBDs) at the N-terminus followed by an arginine-rich region that
is flanked by two short SR (serine/arginine) elements. The RBDs contain the
signatures RDADDA and SWQDLKD found in RBD1 and RBD2 of all typical
metazoan SR proteins. srp2 is essential for growth. We have analyzed in
vivo the role of the modular domains of Srp2 by testing specific mutations
in a conditional strain for complementation. We found that RBD2 is
essential for function and determines the specificity of RBD1 in Srp2.
Replacement of the first RBD with RBD1 of Srp1 of fission yeast does not
change this specificity. The two SR elements in the C-terminus of Srp2 are
also essential for function in vivo. Cellular distribution analysis with
green fluorescence protein fused to portions of Srp2 revealed that the SR
elements are necessary to target Srp2 to the nucleus. Furthermore,
overexpression of modular domains of Srp2 and Srp1 show different effects
on pre-mRNA splicing activity of the tfIId gene. Taken together, these
findings are consistent with the notion that the RBDs of these proteins may
be involved in pre-mRNA recognition.
ARTICLES
Srp2, an SR protein family member of fission yeast: in vivo characterization of its modular domains
Institut fur Genetik-Biozentrum, Technische Universitat Braunschweig, Spielmannstrasse 7, 38106 Braunschweig, Germany.
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