TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 277, No. 33, Issue of August 16, pp. 29654 –29661, 2002 © 2002 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. The Physiological Role of RNase T Can Be Explained by Its Unusual Substrate Specificity* Received for publication, May 1, 2002 Published, JBC Papers in Press, June 5, 2002, DOI 10.1074/jbc.M204252200 Yuhong Zuo and Murray P. Deutscher‡ From the Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101-6129 Escherichia coli RNase T, the enzyme responsible for double-stranded (ds) stem followed by a few unpaired 3
-nu- cleotides (7). 5 S and 23 S rRNAs differ from the other small, the end-turnover of tRNA and for the 3
 maturation of 5 S and 23 S rRNAs and many other small, stable RNAs, stable RNAs in that their mature forms contain only 1 or 2 was examined in detail with respect to its substrate unpaired 3
 residues, whereas the others contain 4 unpaired specificity. The enzyme was found to be a single-strand- residues when matured. Thus, RNase T appears to be the only specific exoribonuclease that acts in the 3
 to 5
 direc- exoribonuclease that 
TI - The Physiological Role of RNase T Can Be Explained by Its Unusual Substrate Specificity
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m204252200
DA - 2002-08-01
UR - https://www.deepdyve.com/lp/unpaywall/the-physiological-role-of-rnase-t-can-be-explained-by-its-unusual-Co1eUq3cRa
DP - DeepDyve
ER -