Sequential assignments and secondary structure of the RNA-binding transcriptional regulator NusB

FEBS Letters

Volumn 415, Issue 2, 1997, Pages 221-226

  Altieri, Amanda S ^a   Mazzulla, Marie J ^a   Zhou, Hongjun ^a   Costantino, Nina ^a   Court, Donald L ^a   Byrd, R Andrew ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Antitermintion; Nuclear magnetic resonance; Nus factor; NusB; RNA binding protein; Secondary structure

Indexed keywords

RNA BINDING PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RNA-BINDING PROTEINS; TRANSCRIPTION FACTORS;

BACTERIOPHAGE LAMBDA;

EID: 0031590311     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01128-9     Document Type: Article

References (63)

1. Das A., Pal M., Garcia-Mena J., Whalen W., Wolska K., Crossley R., Rees W.A., vonHippel P.H., Costantino N., Court D.L., Mazzulla M.J., Altieri A.S., Byrd R.A., Chattopadhyay S., DeVito J., Ghosh B. Methods Enzymol. 274:1996;374-402.
2. Greenblatt, J. (1992) in: Transcriptional Regulation (McKnight, S.L. and Yamamoto, K.R., Eds.) pp. 203-226, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
3. DeVito J., Das A. Proc. Natl. Acad. Sci. USA. 91:1994;8660-8664.
4. Rees W.A., Weitzel S.E., Yager T.D., Das A., von Hippel P.H. Proc. Natl. Acad. Sci. USA. 93:1996;342-346.
5. Mason S.W., Greenblatt J. Genes Dev. 5:1991;1504-1512.
6. Mason S.W., Li J., Greenblatt J. J. Mol. Biol. 223:1992;55-66.
7. Nodwell J.R., Greenblatt J. Cell. 72:1993;261-268.
8. Patterson T.A., Zhang Z., Baker T., Johnson L.L., Friedman D.I., Court D.L. J. Mol. Biol. 236:1994;217-228.
9. Court D.L., Patterson T.A., Baker T., Costantino N., Mao X., Friedman D.I. J. Bacteriol. 177:1995;2589-2591.
10. Burd C.G., Dreyfuss G. Science. 256:1994;615-621.
11. Mattaj I.W. Cell. 73:1993;837-840.
12. Nagai K. Curr. Opin. Struct. Biol. 6:1996;53-61.
13. Swanson M.S., Nakagawa T.Y., LeVan K., Dreyfuss G. Mol. Cell Biol. 7:1987;1731-1739.
14. Oubridge C., Ito N., Evans P.R., Teo C.H., Nagai K. Nature. 372:1994;432-438.
15. Nagai K., Oubridge C., Jessen T.H., Li J., Evans P.R. Nature. 348:1990;515-520.
16. Hoffman D.W., Query C.C., Golden B.L., White S.W., Keene J.D. Proc. Natl. Acad. Sci. USA. 88:1991;2495-2499.
17. Avis J.M., Allain F.H.T., Howe P., Varani G., Nagai K., Neuhaus D. J. Mol. Biol. 257:1996;398-411.
18. Scherly D., Boelens W., Van Venrooij W.J., Dathan N.A., Hamm J., Mattaj I.W. EMBO J. 8:1989;4163-4170.
19. Wittekind M., Gorlach M., Friedrichs M., Dreyfuss G., Mueller L. Biochemistry. 31:1992;6254-6265.
20. Dejgaard K., Leffers H. Eur. J. Biochem. 241:1996;425-431.
21. Musco G., Stier G., Joseph C., Castiglione Morelli M.A., Nilges M., Gibson T.J., Pastore A. Cell. 85:1996;237-245.
22. Kharrat A., Macias M.J., Gibson T.J., Nilges M., Pastore A. EMBO J. 14:1995;3572-3584.
23. Bycroft M., Grunert S., Murzin A.G., Proctor M., St. Johnston D. EMBO J. 14:1995;3563-3571.
24. Pieler, T. (1994) in: RNA-Protein Interactions (Nagai, K. and Mattaj, I.W., Eds.) pp. 178-191, IRL Press, Oxford.
25. Kiledjian M., Dreyfuss G. EMBO J. 11:1992;2655-2664.
26. Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M., Kovar H., Joubert I., deJong P., Rouleau G., Aurias A., Thomas G. Nature. 359:1992;162-165.
27. Lazinski D., Grzadzielska E., Das A. Cell. 59:1989;207-218.
28. Calnan B.J., Biancalana S., Hudson D., Frankel A.D. Genes Dev. 5:1991;201-210.
29. Puglisi J.D., Tan R., Calnan B.J., Frankel A.D., Williamson J.R. Science. 257:1992;76-80.
30. Tan R., Chen L., Buettner J.A., Hudson D., Frankel A.D. Cell. 73:1993;1031-1040.
31. Wolberger C. Curr. Opin. Struct. Biol. 6:1996;62-68.
32. Van Gilst M.R., Rees W.A., Das A., von Hippel P.H. Biochemistry. 36:1997;1514-1524.
33. Bycroft M., Hubbard T.J.P., Proctor M., Freund S.M.V., Murzin A.G. Cell. 88:1997;235-242.
34. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. J. Mol. Biol. 215:1990;403-410.
35. Markus M., Hinck A.P., Huang S., Draper D.E., Torchia D.A. Nat. Struct. Biol. 4:1997;70-77.
36. Xing Y., GuhaThakurta D., Draper D.E. Nat. Struct. Biol. 4:1997;24-27.
37. Berglund H., Rak A., Serganov A., Garber M., Hard T. Nat. Struct. Biol. 4:1997;20-23.
38. Sambrook, J., Fritsch, E.F., Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
39. Grzesiek S., Bax A. J. Am. Chem. Soc. 115:1993;12593-12594.
40. Piotto M., Saudek V., Sklenar V. J. Biomol. NMR. 2:1992;661-665.
41. Altieri A.S., Hinton D.P., Byrd R.A. J. Am. Chem. Soc. 117:1995;7566-7577.
42. Muhandiram D.R., Kay L.E. J. Magn. Reson. Ser. B. 103:1994;203-216.
43. Kraulis P.J. J. Magn. Reson. 84:1989;627-633.
44. Kraulis P.J., Domaille P.J., Campbell-Burke S.L., vanAken T., Laue E.D. Biochemistry. 33:1994;3515-3531.
45. Grzesiek S., Bax A. J. Biomol. NMR. 3:1993;185-204.
46. Kay L.E., Xu G.-Y., Singer A.U., Muhandiram D.R., Foreman-Kay J.D. J. Magn. Reson. Ser. B. 101:1993;333-337.
47. Vuister G.W., Bax A. J. Am. Chem. Soc. 115:1993;7772-7777.
48. Kay L.E., Keifer P., Saarinen T. J. Am. Chem. Soc. 114:1992;10663-10665.
49. Kay L.E., Clore G.M., Bax A., Gronenborn A. Science. 249:1990;411-414.
50. Venters R.A., Metzler W.J., Spicer L.D., Mueller L., Farmer B.T. II. J. Am. Chem. Soc. 117:1995;9592-9593.
51. Grzesiek S., Wingfield P., Stahl S., Kaufman J.D., Bax A. J. Am. Chem. Soc. 117:1995;9594-9595.
52. Greenfield N., Fasman G.D. Biochemistry. 8:1969;4108-4116.
53. Wuthrich, K. (1986) in: NMR of Proteins and Nucleic Acids, John Wiley and Sons, New York, NY.
54. Wishart D.S., Sykes B.D. J. Biomol. NMR. 4:1994;171-180.
55. Spera S., Bax A. J. Am. Chem. Soc. 113:1991;5490-5492.
56. Wishart D.S., Sykes B.D., Richards F.M. Biochemistry. 31:1992;1647-1651.
57. Rost, B. (1996) Methods Enzymol. 266, 525-539; Rost, B. and Sander, S. (1993) J. Mol. Biol. 232, 584-599; Rost, B. and Sander, S. (1994) Proteins 19, 55-72. The secondary structure prediction program PHDsec calculated NusB to contain 81.3% α-helix.
58. Rost, B. (1996) Methods Enzymol. 266, 525-539; Rost, B. and Sander, S. (1993) J. Mol. Biol. 232, 584-599; Rost, B. and Sander, S. (1994) Proteins 19, 55-72. The secondary structure prediction program PHDsec calculated NusB to contain 81.3% α-helix.
59. Rost, B. (1996) Methods Enzymol. 266, 525-539; Rost, B. and Sander, S. (1993) J. Mol. Biol. 232, 584-599; Rost, B. and Sander, S. (1994) Proteins 19, 55-72. The secondary structure prediction program PHDsec calculated NusB to contain 81.3% α-helix.
60. Chattopadhyay S., Hung S.C., Stuart A.C., Palmer A.G. III, Garcia-Mena J., Das A., Gottesman M.E. Proc. Natl. Acad. Sci. USA. 92:1995;12131-12135.
61. Varani G. Acc. Chem. Res. 30:1997;189-195.
62. Marion D., Ikura M., Tschudin R., Bax A. J. Magn. Reson. 85:1989;393-399.
63. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. 6:1995;277-293.