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Gene Review

ECs2513  -  ribonuclease D

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs2513

  • Similarly, RNase D action on the E. coli tRNATyr precursor is limited, whereas RNase II causes extensive degradation [1].
  • Moreover, three recombinant HIV-1 RT preparations expressed and purified in different laboratories by various procedures exhibit RNase D activity [2].
  • We refer to this unusual activity as RNase D. Two lines of evidence indicate that the specific RNase D activity is an integral part of recombinant HIV RT [2].
  • The implications of these findings for the role of RNase D in bacterial and bacteriophage tRNA metabolism, and the possible involvement of alternative enzymes, are discussed [3].

High impact information on ECs2513

  • Alteration of two to five uridine residues within this sequence has no effect on mRNA levels but decreases RNase D protein and activity by as much as 95%, indicating that the U-rich sequence acts as an enhancer of translation [4].
  • A new ribonuclease, RNase BN, has been identified and partially purified from a strain of Escherichia coli lacking RNase II and RNase D by using the artificial tRNA precursor tRNA-C-[14C]U as substrate [5].
  • In contrast to the processive mode of hydrolysis by RNase II, RNase D removes nucleotides randomly and slows down greatly at the -C-C-A sequence, thereby allowing the tRNA to be aminoacylated and protected from further degradation [1].
  • This alteration led to an 11-fold elevation of RNase D expression in single-copy plasmids [6].
  • However, since mutant Escherichia coli strains devoid of RNase D display a normal phenotype, it has not been possible to ascertain the enzyme's function or even to determine which RNA is its substrate in vivo [7].

Biological context of ECs2513


Associations of ECs2513 with chemical compounds

  • A variety of RNAs were tested as substrates for RNase D. Alteration of the 3'-terminal base has no effect on the rate of hydrolysis, whereas modification of the 3'-terminal sugar has a major effect. tRNA terminating with a 3'-phosphate is completely inactive as a substrate [8].

Other interactions of ECs2513

  • Studies of the mode of action of RNase D indicate that it is an exonuclease which initiates hydrolysis at the 3'-terminus and removes 5'-mononucleotides in a random fashion [8].

Analytical, diagnostic and therapeutic context of ECs2513

  • Surprisingly, deletion of the hairpin structure elevates rnd mRNA levels only slightly (less than 2-fold), but it dramatically decreases RNase D expression (greater than 95%), measured both by activity and immunoblotting [6].


  1. Apparent involvement of ribonuclease D in the 3' processing of tRNA precursors. Cudny, H., Deutscher, M.P. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  2. Double-stranded RNA-dependent RNase activity associated with human immunodeficiency virus type 1 reverse transcriptase. Ben-Artzi, H., Zeelon, E., Gorecki, M., Panet, A. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  3. Ribonuclease D is not essential for the normal growth of Escherichia coli or bacteriophage T4 or for the biosynthesis of a T4 suppressor tRNA. Blouin, R.T., Zaniewski, R., Deutscher, M.P. J. Biol. Chem. (1983) [Pubmed]
  4. A uridine-rich sequence required for translation of prokaryotic mRNA. Zhang, J., Deutscher, M.P. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme. Asha, P.K., Blouin, R.T., Zaniewski, R., Deutscher, M.P. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  6. Analysis of the upstream region of the Escherichia coli rnd gene encoding RNase D. Evidence for translational regulation of a putative tRNA processing enzyme. Zhang, J.R., Deutscher, M.P. J. Biol. Chem. (1989) [Pubmed]
  7. Transfer RNA is a substrate for RNase D in vivo. Zhang, J.R., Deutscher, M.P. J. Biol. Chem. (1988) [Pubmed]
  8. Escherichia coli RNase D. Catalytic properties and substrate specificity. Cudny, H., Zaniewski, R., Deutscher, M.P. J. Biol. Chem. (1981) [Pubmed]
  9. Escherichia coli RNase D: sequencing of the rnd structural gene and purification of the overexpressed protein. Zhang, J.R., Deutscher, M.P. Nucleic Acids Res. (1988) [Pubmed]
  10. Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing. Zuo, Y., Wang, Y., Malhotra, A. Structure (Camb.) (2005) [Pubmed]
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