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Mol Cell Biol, April 1998, p. 1956-1966, Vol. 18, No. 4
CNRS UPR 9005, 67000 Strasbourg,
France,1 and
EMBL, D-69117
Heidelberg, Germany2
Received 22 August 1997/Returned for modification 14 October
1997/Accepted 21 January 1998
Sm core proteins play an essential role in the formation of
small nuclear ribonucleoprotein particles (snRNPs) by binding to
small nuclear RNAs and participating in a network of protein interactions. The two-hybrid system was used to identify SmE
interacting proteins and to test for interactions between all pairwise
combinations of yeast Sm proteins. We observed interactions between SmB
and SmD3, SmE and SmF, and SmE and SmG. For these interactions, a direct biochemical assay confirmed the validity of the results obtained
in vivo. To map the protein-protein interaction surface of Sm proteins,
we generated a library of SmE mutants and investigated their ability to
interact with SmF and/or SmG proteins in the two-hybrid system. Several
classes of mutants were observed: some mutants are unable to interact
with either SmF or SmG proteins, some interact with SmG but not with
SmF, while others interact moderately with SmF but not with SmG. Our
mutational analysis of yeast SmE protein shows that conserved
hydrophobic residues are essential for interactions with SmF and SmG as
well as for viability. Surprisingly, we observed that other
evolutionarily conserved positions are tolerant to mutations, with
substitutions affecting binding to SmF and SmG only mildly and
conferring a wild-type growth phenotype.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Interactions within the Yeast Sm Core Complex:
from Proteins to Amino Acids
*
Corresponding author. Mailing address: CNRS UPR 9005, 15 rue René Descartes, 67000 Strasbourg, France. Phone: 33 3 88 45 46 44. Fax: 33 3 88 41 70 70. E-mail:
bordonne{at}ibmc.u-strasbg.fr.
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