The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ECs2513  -  ribonuclease D

Escherichia coli O157:H7 str. Sakai

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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].

References

  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]
 
WikiGenes - Universities