Catalytic properties of RNase BN/RNase Z from Escherichia coli. RNase BN is both an exo- and endoribonuclease

Journal of Biological Chemistry

Volumn 284, Issue 23, 2009, Pages 15425-15431

  Dutta, Tanmay ^a   Deutscher, Murray P ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC POTENTIAL; CATALYTIC PROPERTIES; DIGESTION PRODUCTS; ENDORIBONUCLEASE; EUBACTERIA; MONONUCLEOTIDES; PHOSPHORYL GROUPS; POTENTIAL SUBSTRATE; RNA MOLECULES; RNASE Z; SYNTHETIC SUBSTRATES; TRNA GENES;

ESCHERICHIA COLI; NUCLEIC ACIDS; NUCLEOTIDES; RNA; SUBSTRATES;

ENZYMES;

DOUBLE STRANDED RNA; EXORIBONUCLEASE; PHOSPHODIESTERASE; RIBONUCLEASE; RIBONUCLEASE BN; RIBONUCLEASE Z; RIBONUCLEOTIDE; SINGLE STRANDED RNA; UNCLASSIFIED DRUG; BACTERIAL RNA; DIVALENT CATION; ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN; RNASE Z; TRANSFER RNA;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; RNA CLEAVAGE; TERMINAL SEQUENCE; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

BASE SEQUENCE; CATIONS, DIVALENT; ENDORIBONUCLEASES; ESCHERICHIA COLI PROTEINS; EXORIBONUCLEASES; KINETICS; PHOSPHORIC DIESTER HYDROLASES; RECOMBINANT PROTEINS; RNA, BACTERIAL; RNA, TRANSFER; SUBSTRATE SPECIFICITY;

EID: 67650156456     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.005462     Document Type: Article

References (32)

1. Deutscher, M. P. (1995) in tRNA: Structure, Biosynthesis, and Function (Soll, D., and Rajbhandary, U. L., eds) pp. 51-65, American Society for Microbiology, Washington, D.C.
2. Deutscher, M. P. (1990) Prog. Nucleic Acid Res. Mol. Biol. 39, 209-240
3. Vogel, A., Schilling, O., Späth, B., and Marchfelder, A. (2005) Biol. Chem. 386, 1253-1264
4. Schierling, K., Rösch, S., Rupprecht, R., Schiffer, S., and Marchfelder, A. (2002) J. Mol. Biol. 316, 895-902
5. Redko, Y., de la Sierra-Gallay, I. L., and Condon, C. (2007) Nat. Rev. Microbiol. 5, 278-286
6. Minagawa, A., Takaku, H., Takagi, M., and Nashimoto, M. (2004) J. Biol. Chem. 279, 15688-15697
7. Li, Z., and Deutscher, M. P. (1996) Cell 86, 503-512
8. Reuven, N. B., and Deutscher, M. P. (1993) FASEB J. 7, 143-148
9. Schiffer, S., Rösch, S., and Marchfelder, A. (2002) EMBO J. 21, 2769-2777
10. Weiner, A. M. (2004) Curr. Biol. 14, 883-885
11. Vogel, A., Schilling, O., Niecke, M., Bettmer, J., and Meyer-Klaucke, W. (2002) J. Biol. Chem. 277, 29078-29085
12. Schilling, O., Rüggeberg, S., Vogel, A., Rittner, N., Weichert, S., Schmidt, S., Doig, S., Franz, T., Benes, V., Andrews, S. C., Baum, M., and Meyer-Klaucke, W. (2004) Biochem. Biophys. Res. Commun. 320, 1365-1373
13. Ezraty, B., Dahlgren, B., and Deutscher, M. P. (2005) J. Biol. Chem. 280, 16542-16545
14. Schilling, O., Späth, B., Kostelecky, B., Marchfelder, A., Meyer-Klaucke, W., and Vogel, A. (2005) J. Biol. Chem. 280, 17857-17862
15. Asha, P. K., Blouin, R. T., Zaniewski, R., and Deutscher, M. P. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 3301-3304
16. Seidman, J. G., Schmidt, F. J., Foss, K., and McClain, W. H. (1975) Cell 5, 389-400
17. Deutscher, M. P. (1993) J. Bacteriol. 175, 4577-4583
18. Elbarbary, R. A., Takaku, H., and Nashimoto, M. (2008) Biochim. Biophys. Acta 1784, 2079-2085
19. Kelly, K. O., and Deutscher, M. P. (1992) J. Bacteriol. 174, 6682-6684
20. Shibata, H. S., Minagawa, A., Takaku, H., Takagi, M., and Nashimoto, M. (2006) Biochemistry 45, 5486-5492
21. Uziel, M. (1973) Biochemistry 12, 938-942
22. Pellegrini, O., Nezzar, J., Marchfelder, A., Putzer, H., and Condon, C. (2003) EMBO J. 22, 4534-4543
23. Mohan, A., Whyte, S., Wang, X., Nashimoto, M., and Levinger, L. (1999) RNA 5, 245-256
24. de la Sierra-Gallay, I. L., Pellegrini, O., and Condon, C. (2005) Nature 433, 657-661
25. Zareen, N., Hopkinson, A., and Levinger, L. (2006) RNA 12, 1104-1115
26. Kostelecky, B., Pohl, E., Vogel, A., Schilling, O., and Meyer-Klaucke, W. (2006) J. Bacteriol. 188, 1607-1614
27. de la Sierra-Gallay, I. L., Mathy, N., Pellegrini, O., and Condon, C. (2006) Nat. Struct. Mol. Biol. 13, 376-377
28. Schiffer, S., Rösch, S., and Marchfelder, A. (2003) Biol. Chem. 384, 333-342
29. Takaku, H., and Nashimoto, M. (2008) Genes Cells 13, 1087-1097
30. Perwez, T., and Kushner, S. R. (2006) Mol. Microbiol. 60, 723-737
31. de la Sierra-Gallay, I. L., Zig. L., Jamalli, A., and Putzer, H. (2008) Nat. Struct. Mol. Biol. 15, 206-212
32. Yang, X. C., Sullivan, K. D., Marzluff, W. F., and Dominski, Z. (2009) Mol. Cell. Biol. 29, 31-42