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Volume 272, Number 26,
Issue of June 27, 1997
pp. 16103-16109
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Ssd1p of Saccharomyces cerevisiae Associates with
RNA
(Received for publication, April 25, 1997)
Yukifumi
Uesono
,
Akio
Toh-e
and
Yoshiko
Kikuchi
From the Department of Biological Sciences, Graduate School of
Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku,
Tokyo 113, Japan
The SSD1 gene has been isolated as a
single copy suppressor of many mutants, such as sit4,
slk1/bck1, pde2, and rpc31, in the
yeast Saccharomyces cerevisiae. Ssd1p has domains showing weak but significant homology with RNase II-related proteins, Cyt4p,
Dss1p, VacB, and RNase II, which are involved in the modification of
RNA. We found that Ssd1p had the ability to bind RNA, preferably poly(rA), as well as single-stranded DNA. Interestingly, the most conserved domain among the RNase II-related proteins was not necessary for interaction with RNA. Indirect immunofluorescence staining with
anti-Ssd1p antibody revealed that Ssd1p was detected mainly in the
cytoplasm. Furthermore, sucrose gradient sedimentation analysis
demonstrated that Ssd1p was not cofractionated with polyribosomes, suggesting that Ssd1p is not particularly bound to a translationally active subpopulation of mRNA in the cytoplasm.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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