Species-Specific Cleavage by RNase E-Like Enzymes in 5S rRNA Maturation
2005
Ryou, S.M. (Chung-Ang University, Seoul, Republic of Korea) | Kim, J.M. (Chung-Ang University, Seoul, Republic of Korea) | Yeom, J.H. (Chung-Ang University, Seoul, Republic of Korea) | Kim, H.L. (Chung-Ang University, Seoul, Republic of Korea) | Go, H.Y. (Chung-Ang University, Seoul, Republic of Korea) | Shin, E.K. (Chung-Ang University, Seoul, Republic of Korea) | Lee, K.S. (Chung-Ang University, Seoul, Republic of Korea), E-mail: kangseok@cau.ac.kr
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.
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