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Gene Review

UTI89_C1284  -  N protein

Escherichia coli UTI89

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Disease relevance of UTI89_C1284

  • The fourth nucleotide of the loop extrudes from the GNRA fold to enable the E. coli elongation factor NusA to recognize the N protein/RNA complex [1].
  • As a transcriptional activator, the N protein of phage lambda acts to suppress transcription termination by recognizing a promoter-proximal site, nut, which is separated from the terminators by thousands of base pairs [2].
  • In this study, recombinant SARS-CoV N protein was shown to be dimeric by analytical ultracentrifugation, size exclusion chromatography coupled with light scattering, and chemical cross-linking [3].
  • These results suggest that the N protein oligomerization involves the C-terminal residues 285-422, and this region is a good target for mutagenic studies to disrupt N protein self-association and virion assembly [3].
  • We have purified the Rhodobacter capsulatus sigma N protein, which is distinctive in lacking an acidic region implicated in the melting of promoter DNA by the Escherichia coll sigma N holoenzyme, and may represent a minor subclass of sigma N proteins [4].

High impact information on UTI89_C1284


Chemical compound and disease context of UTI89_C1284


Biological context of UTI89_C1284


Anatomical context of UTI89_C1284


Associations of UTI89_C1284 with chemical compounds


Physical interactions of UTI89_C1284


Other interactions of UTI89_C1284

  • We discuss whether nusB is specific for N protein or for some other component of this regulation system, e.g. the phage site (nut) required for N action [25].

Analytical, diagnostic and therapeutic context of UTI89_C1284


  1. NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif. Legault, P., Li, J., Mogridge, J., Kay, L.E., Greenblatt, J. Cell (1998) [Pubmed]
  2. An antitermination protein engages the elongating transcription apparatus at a promoter-proximal recognition site. Barik, S., Ghosh, B., Whalen, W., Lazinski, D., Das, A. Cell (1987) [Pubmed]
  3. Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain. Yu, I.M., Gustafson, C.L., Diao, J., Burgner, J.W., Li, Z., Zhang, J., Chen, J. J. Biol. Chem. (2005) [Pubmed]
  4. Purification and activities of the Rhodobacter capsulatus RpoN (sigma N) protein. Cannon, W., Missailidis, S., Austin, S., Moore, M., Drake, A., Buck, M. Mol. Microbiol. (1996) [Pubmed]
  5. Protein degradation in E. coli: the Ion mutation and bacteriophage lambda N and cll protein stability. Gottesman, S., Gottesman, M., Shaw, J.E., Pearson, M.L. Cell (1981) [Pubmed]
  6. The RNA-protein complex: direct probing of the interfacial recognition dynamics and its correlation with biological functions. Xia, T., Becker, H.C., Wan, C., Frankel, A., Roberts, R.W., Zewail, A.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. Analysis of nutR, a site required for transcription antitermination in phage lambda. Zuber, M., Patterson, T.A., Court, D.L. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  8. Isolation and characterization of conditional-lethal rho mutants of Escherichia coli. Inoko, H., Shigesada, K., Imai, M. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  9. Host factor requirements for processive antitermination of transcription and suppression of pausing by the N protein of bacteriophage lambda. Mason, S.W., Li, J., Greenblatt, J. J. Biol. Chem. (1992) [Pubmed]
  10. Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli. Maurizi, M.R. J. Biol. Chem. (1987) [Pubmed]
  11. Adenosine triphosphate-dependent degradation of a fluorescent lambda N substrate mimic by Lon protease. Lee, I., Berdis, A.J. Anal. Biochem. (2001) [Pubmed]
  12. Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex. Schärpf, M., Sticht, H., Schweimer, K., Boehm, M., Hoffmann, S., Rösch, P. Eur. J. Biochem. (2000) [Pubmed]
  13. Transcription antitermination: the lambda paradigm updated. Friedman, D.I., Court, D.L. Mol. Microbiol. (1995) [Pubmed]
  14. Respiratory syncytial virus M2-1 protein requires phosphorylation for efficient function and binds viral RNA during infection. Cartee, T.L., Wertz, G.W. J. Virol. (2001) [Pubmed]
  15. lambda N antitermination system: functional analysis of phage interactions with the host NusA protein. Schauer, A.T., Carver, D.L., Bigelow, B., Baron, L.S., Friedman, D.I. J. Mol. Biol. (1987) [Pubmed]
  16. Evidence that the KH RNA-binding domains influence the action of the E. coli NusA protein. Zhou, Y., Mah, T.F., Greenblatt, J., Friedman, D.I. J. Mol. Biol. (2002) [Pubmed]
  17. Characterization of the nucleic acid binding properties of tomato spotted wilt virus nucleocapsid protein. Richmond, K.E., Chenault, K., Sherwood, J.L., German, T.L. Virology (1998) [Pubmed]
  18. Immune responses against SARS-coronavirus nucleocapsid protein induced by DNA vaccine. Zhao, P., Cao, J., Zhao, L.J., Qin, Z.L., Ke, J.S., Pan, W., Ren, H., Yu, J.G., Qi, Z.T. Virology (2005) [Pubmed]
  19. Utilization of autopsy RNA for the synthesis of the nucleocapsid antigen of a newly recognized virus associated with hantavirus pulmonary syndrome. Feldmann, H., Sanchez, A., Morzunov, S., Spiropoulou, C.F., Rollin, P.E., Ksiazek, T.G., Peters, C.J., Nichol, S.T. Virus Res. (1993) [Pubmed]
  20. Antitermination of transcription by the N-gene protein of bacteriophage lambda: recent progress and remaining problems. Greenblatt, J. Ann. Microbiol. (Paris) (1982) [Pubmed]
  21. Purification and characterization of herpes simplex virus (type 1) thymidine kinase produced in Escherichia coli by a high efficiency expression plasmid utilizing a lambda PL promoter and cI857 temperature-sensitive repressor. Waldman, A.S., Haeusslein, E., Milman, G. J. Biol. Chem. (1983) [Pubmed]
  22. Antigenic properties and diagnostic potential of puumala virus nucleocapsid protein expressed in insect cells. Vapalahti, O., Lundkvist, A., Kallio-Kokko, H., Paukku, K., Julkunen, I., Lankinen, H., Vaheri, A. J. Clin. Microbiol. (1996) [Pubmed]
  23. Solubility, immunogenicity and physical properties of the nucleocapsid protein of Nipah virus produced in Escherichia coli. Tan, W.S., Ong, S.T., Eshaghi, M., Foo, S.S., Yusoff, K. J. Med. Virol. (2004) [Pubmed]
  24. Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda. Chattopadhyay, S., Garcia-Mena, J., DeVito, J., Wolska, K., Das, A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  25. Escherichia coli nusB mutations that suppress nusA1 exhibit lambda N specificity. Ward, D.F., DeLong, A., Gottesman, M.E. J. Mol. Biol. (1983) [Pubmed]
  26. A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein. Mogridge, J., Mah, T.F., Greenblatt, J. Genes Dev. (1995) [Pubmed]
  27. Study of the assembly of vesicular stomatitis virus N protein: role of the P protein. Green, T.J., Macpherson, S., Qiu, S., Lebowitz, J., Wertz, G.W., Luo, M. J. Virol. (2000) [Pubmed]
  28. Detection of antibodies to U.S. isolates of avian pneumovirus by a recombinant nucleocapsid protein-based sandwich enzyme-linked immunosorbent assay. Gulati, B.R., Munir, S., Patnayak, D.P., Goyal, S.M., Kapur, V. J. Clin. Microbiol. (2001) [Pubmed]
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