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Species-Specific Cleavage by RNase E-Like Enzymes in 5S rRNA Maturation  

RYOU SANG-MI (Department of Life Science, Chung-Ang University)
KIM JONG-MYUNG (Department of Life Science, Chung-Ang University)
YEOM JI-HYUN (Department of Life Science, Chung-Ang University)
KIM HYUN-LI (Department of Life Science, Chung-Ang University)
GO HA-YOUNG (Department of Life Science, Chung-Ang University)
SHIN EUN-KYOUNG (Department of Life Science, Chung-Ang University)
LEE KANGSEOK (Department of Life Science, Chung-Ang University)
Publication Information
Journal of Microbiology and Biotechnology / v.15, no.5, 2005 , pp. 1100-1105 More about this Journal
Abstract
Previous work has identified a Streptomyces coelicolor gene, rns, encoding a 140 kDa protein (RNase ES) that exhibits the endoribonucleolytic cleavage specificity characteristic of RNase E and confers viability on and allows the propagation of E. coli cells lacking RNase E. Here, we identify a putative S. coelicolor 9S rRNA sequence and sites cleaved by RNase ES. The cleavage of the S. coelicolor 9S rRNA transcript by RNase ES resulted in a 5S rRNA precursor (p5S) that had four and two additional nucleotides at the 5' end and 3' ends of the mature 5S rRNA, respectively. However, despite the similarities between RNase E and RNase ES, these enzymes could accurately process 9S rRNA from just their own bacteria, indicating that these ancient enzymes and the rRNA segments that they attack appear to have co-evolved.
Keywords
RNase E; RNase ES; 9S rRNA; 5S rRNA; p5S; RNA processing;
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