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MOLECULAR AND CELLULAR BIOLOGY, 0270-7306/00/$04.00 0
 

Summary: MOLECULAR AND CELLULAR BIOLOGY,
0270-7306/00/$04.00 0
Feb. 2000, p. 1104­1115 Vol. 20, No. 4
Copyright © 2000, American Society for Microbiology. All Rights Reserved.
The N-Terminal Domain That Distinguishes Yeast from
Bacterial RNase III Contains a Dimerization Signal Required
for Efficient Double-Stranded RNA Cleavage
BRUNO LAMONTAGNE, ANNIE TREMBLAY, AND SHERIF ABOU ELELA*
De´partement de Microbiologie et d'Infectiologie, Faculte´ de Me´decine, Universite´ de Sherbrooke,
Sherbrooke, Que´bec, Canada J1H 5N4
Received 1 September 1999/Returned for modification 18 October 1999/Accepted 17 November 1999
Yeast Rnt1 is a member of the double-stranded RNA (dsRNA)-specific RNase III family identified by
conserved dsRNA binding (dsRBD) and nuclease domains. Comparative sequence analyses have revealed an
additional N-terminal domain unique to the eukaryotic homologues of RNase III. The deletion of this domain
from Rnt1 slowed growth and led to mild accumulation of unprocessed 25S pre-rRNA. In vitro, deletion of the
N-terminal domain reduced the rate of RNA cleavage under physiological salt concentration. Size exclusion
chromatography and cross-linking assays indicated that the N-terminal domain and the dsRBD self-interact
to stabilize the Rnt1 homodimer. In addition, an interaction between the N-terminal domain and the dsRBD
was identified by a two-hybrid assay. The results suggest that the eukaryotic N-terminal domain of Rnt1
ensures efficient dsRNA cleavage by mediating the assembly of optimum Rnt1-RNA ribonucleoprotein complex.

  

Source: Abou Elela, Sherif - Département de Microbiologie et d'Infectiologie, Université de Sherbrooke

 

Collections: Biology and Medicine