학술논문

Imp3p and lmp4p mediate formation of essential U3 -- precursor rRNA (pre-rRNA) duplexes, possibly to recruit the small subunit processome to the pre-rRNA.
Document Type
Article
Source
Proceedings of the National Academy of Sciences of the United States of America. 10/26/2004, Vol. 101 Issue 43, p15301-15306. 6p.
Subject
*RNA
*ORIGIN of life
*PROTEIN precursors
*SACCHAROMYCES cerevisiae
*EUKARYOTIC cells
*SACCHAROMYCES
*SMALL subunit processomes
Language
ISSN
0027-8424
Abstract
In eukaryotes, formation of short duplexes between the U3 small nucleolar RNA (snoRNA) and the precursor rRNA (pre-rRNA) at multiple sites is a prerequisite for three endonucleolytic cleavages that initiate small subunit biogenesis by releasing the 185 rRNA precursor from the pre-rRNA. The most likely role of these RNA duplexes is to guide the U3 snoRNA and its associated proteins, designated the small subunit processome, to the target cleavage sites on the pre-rRNA. Studies by others in Saccharomyces cerevisiae have identified the proteins Mpp10p, lmp3p, and lmp4p as candidates to mediate U3-pre-rRNA interactions. We report here that lmp3p and lmp4p appear to stabilize an otherwise unstable duplex between the U3 snoRNA hinge region and complementary bases in the external transcribed spacer of the pre-rRNA. In addition, lmp4p, but not lmp3p, seems to rearrange the U3 box A stem structure to expose the site that base-pairs with the 5' end of the 185 rRNA, thereby mediating duplex formation at a second site. By mediating formation of both essential U3-pre-rRNA duplexes, lmp3p and lmp4p may help the small subunit processome to dock onto the pre-rRNA, an event indispensable for ribosome biogenesis and hence for cell growth. [ABSTRACT FROM AUTHOR]