![]()
|
|
||||||||
J Biol Chem, Vol. 275, Issue 2, 1030-1034, January 14, 2000
,
From the RNase BN, a tRNA-processing enzyme previously
shown to be required for the 3'-maturation of certain bacteriophage
T4-encoded tRNAs, was overexpressed and purified to near homogeneity
from Escherichia coli. The purified enzyme, which is free
of nucleic acid, is an
Department of Biochemistry and Molecular
Biology, University of Miami School of Medicine, Miami, Florida
33101-6129 and the § Department of Biochemistry, University
of Connecticut Health Center, Farmington, Connecticut 06032
2-dimer with a molecular mass of
~65 kDa. RNase BN displays a number of unusual catalytic properties
compared with the other exoribonucleases of E. coli. The
enzyme is most active at pH 6.5 in the presence of Co2+ and
high concentrations of monovalent salts. It is highly specific for tRNA
substrates containing an incorrect residue within the universal 3'-CCA
sequence. Thus, tRNA-CU and tRNA-CA are effective substrates, whereas
intact tRNA-CCA, elongated tRNA-CCA-Cn, phosphodiesterase-treated tRNA,
and the closely related tRNA-CC are essentially inactive as substrates.
RNA or DNA oligonucleotides also are not substrates. These data
indicate that RNase BN has an extremely narrow substrate specificity.
However, since tRNA molecules with incorrect residues within the -CCA
sequence are not normally produced in E. coli, the role of
RNase BN in uninfected cells remains to be determined.
To whom correspondence should be addressed. Tel.:
305-243-3150; Fax: 305-243-3955; E-mail: mdeutsch@med.miami.edu.
This article has been cited by other articles:
![]() |
L. Musumeci, C. Bongiorni, L. Tautz, R. A. Edwards, A. Osterman, M. Perego, T. Mustelin, and N. Bottini Low-Molecular-Weight Protein Tyrosine Phosphatases of Bacillus subtilis J. Bacteriol., July 15, 2005; 187(14): 4945 - 4956. [Abstract] [Full Text] [PDF] |
||||
![]() |
I. A. Oussenko, R. Sanchez, and D. H. Bechhofer Bacillus subtilis YhaM, a Member of a New Family of 3'-to-5' Exonucleases in Gram-Positive Bacteria J. Bacteriol., November 15, 2002; 184(22): 6250 - 6259. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Zuo and M. P. Deutscher Exoribonuclease superfamilies: structural analysis and phylogenetic distribution Nucleic Acids Res., March 1, 2001; 29(5): 1017 - 1026. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |