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PBRM1  -  polybromo 1

Homo sapiens

Synonyms: BAF180, BRG1-associated factor 180, PB1, Polybromo-1D, Protein polybromo-1, ...
 
 
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Disease relevance of PBRM1

 

High impact information on PBRM1

  • The selectivity by PBAF requires a novel subunit, BAF200, but not the previously described PBAF-specificity subunit, BAF180 (Polybromo) [4].
  • The PB1 domain and the PC motif-containing region are structurally similar protein binding modules [5].
  • Endonuclease cleavage, which is activated by the subsequent binding of the 3' terminal sequence of vRNA, resides in a PB1 sequence that contains three essential acidic amino acids, similar to the active sites of other enzymes that cut polynucleotides to produce 3'-OH ends [6].
  • We report here the NMR structure and ligand-binding site of the PB1 domain of the cell polarity establishment protein, Bem1p [7].
  • The chemical shift perturbation experiment and the mutagenesis study show that the PC motif is a major structural element that binds to the PB1 domain [7].
 

Chemical compound and disease context of PBRM1

  • Despite being isolated within a single year in the same geographical location, human H5N1 viruses were characterized by a variety of amino acid substitutions in the ribonucleoprotein complex [PB2, PB1, PA and nucleoprotein (NP)] as well as the matrix (M) proteins 1 and 2 and nonstructural (NS) proteins 1 and 2 [8].
  • We have demonstrated that 5'-capped short RNA fragments inhibit the expression of chloramphenicol acetyltransferase (CAT) in the murine 76 cell line, derived which expresses the genes for the RNA polymerases (PB1, PB2, and PA) and the nucleoprotein (NP) of influenza virus in response to treatment with dexamethasone [9].
  • In this study, we obtained partial gene sequences of 4 genes (PB1-like protein, PA-like protein, glycoprotein, and nucleoprotein) of 8 Thogoto virus strains isolated in Africa, Asia, and Europe and studied the genetic variation and phylogeny [10].
 

Biological context of PBRM1

 

Anatomical context of PBRM1

 

Associations of PBRM1 with chemical compounds

  • In addition to the PB2 protein subunit acquiring the ability to bind 5'-capped ends of RNAs, the PB1 protein itself acquires the ability to bind the 3' sequence of vRNA, via a ribonucleoprotein 1 (RNP1)-like motif, amino acids 249-256, which contains two phenylalanine residues required for binding [18].
  • On the interface, several salt bridges are formed including the conserved acidic residues on the OPCA motif of PKCiota PB1 and the conserved lysine residue on the Par6alpha PB1 [19].
  • Sucrose density gradient analysis showed that the P protein complexes ranged from about 11S to 22S and that almost all of the PB1 and PB2 protein molecules synthesized during a 1-h period (2.5 to 3.5 h postinfection) were in these complexes [20].
  • Mutant PAS509, which had a serine insertion at position 509, bound to PB1 like wild-type PA but did not show any polymerase activity [21].
  • The neuraminidase (NA) and PB1 genes of the H1N2 isolate were of human origin, while the hemagglutinin (HA), matrix (M), nucleoprotein (NP), and non-structural (NS) genes were of swine origin and PA and PB2 gene were of avain origin [22].
 

Other interactions of PBRM1

  • Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice [23].
  • This paper recalls the reasons why growth models are useful, analyses briefly the structure and the characteristics of the two fundamental human growth functions, i.e. triple-logistic and PB1, and shows how the use of PB1 model may be extended also to impaired growth, e.g. in girls with Turner syndrome [24].
 

Analytical, diagnostic and therapeutic context of PBRM1

References

  1. The 3p21 candidate tumor suppressor gene BAF180 is normally expressed in human lung cancer. Sekine, I., Sato, M., Sunaga, N., Toyooka, S., Peyton, M., Parsons, R., Wang, W., Gazdar, A.F., Minna, J.D. Oncogene (2005) [Pubmed]
  2. cDNA cloning of the human polybromo-1 gene on chromosome 3p21. Horikawa, I., Barrett, J.C. DNA Seq. (2002) [Pubmed]
  3. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. Hara, K., Schmidt, F.I., Crow, M., Brownlee, G.G. J. Virol. (2006) [Pubmed]
  4. PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes. Yan, Z., Cui, K., Murray, D.M., Ling, C., Xue, Y., Gerstein, A., Parsons, R., Zhao, K., Wang, W. Genes Dev. (2005) [Pubmed]
  5. The PB1 domain and the PC motif-containing region are structurally similar protein binding modules. Yoshinaga, S., Kohjima, M., Ogura, K., Yokochi, M., Takeya, R., Ito, T., Sumimoto, H., Inagaki, F. EMBO J. (2003) [Pubmed]
  6. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. Li, M.L., Rao, P., Krug, R.M. EMBO J. (2001) [Pubmed]
  7. Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. Terasawa, H., Noda, Y., Ito, T., Hatanaka, H., Ichikawa, S., Ogura, K., Sumimoto, H., Inagaki, F. EMBO J. (2001) [Pubmed]
  8. Evolutionary characterization of the six internal genes of H5N1 human influenza A virus. Hiromoto, Y., Yamazaki, Y., Fukushima, T., Saito, T., Lindstrom, S.E., Omoe, K., Nerome, R., Lim, W., Sugita, S., Nerome, K. J. Gen. Virol. (2000) [Pubmed]
  9. Inhibition of influenza virus RNA polymerase by 5'-capped short RNA fragments. Hatta, T., Ishikawa, M., Takai, K., Nakada, S., Yokota, T., Hata, T., Miura, K., Takaku, H. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  10. Phylogeny of Thogoto virus. Kuno, G., Chang, G.J., Tsuchiya, K.R., Miller, B.R. Virus Genes (2001) [Pubmed]
  11. Expression, purification and characterization of individual bromodomains from human Polybromo-1. Chandrasekaran, R., Thompson, M. Protein Expr. Purif. (2006) [Pubmed]
  12. The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes. Xue, Y., Canman, J.C., Lee, C.S., Nie, Z., Yang, D., Moreno, G.T., Young, M.K., Salmon, E.D., Wang, W. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  13. Largest subunits of the human SWI/SNF chromatin-remodeling complex promote transcriptional activation by steroid hormone receptors. Inoue, H., Furukawa, T., Giannakopoulos, S., Zhou, S., King, D.S., Tanese, N. J. Biol. Chem. (2002) [Pubmed]
  14. The PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages. Coleman, J.R. Virol. J. (2007) [Pubmed]
  15. Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions. Ito, T., Matsui, Y., Ago, T., Ota, K., Sumimoto, H. EMBO J. (2001) [Pubmed]
  16. Activation of the granulocyte-macrophage colony-stimulating factor promoter in T cells requires cooperative binding of Elf-1 and AP-1 transcription factors. Wang, C.Y., Bassuk, A.G., Boise, L.H., Thompson, C.B., Bravo, R., Leiden, J.M. Mol. Cell. Biol. (1994) [Pubmed]
  17. A spindle checkpoint arrest and a cytokinesis failure by the dominant-negative polo-box domain of Plk1 in U-2 OS cells. Seong, Y.S., Kamijo, K., Lee, J.S., Fernandez, E., Kuriyama, R., Miki, T., Lee, K.S. J. Biol. Chem. (2002) [Pubmed]
  18. RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites. Li, M.L., Ramirez, B.C., Krug, R.M. EMBO J. (1998) [Pubmed]
  19. Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. Hirano, Y., Yoshinaga, S., Takeya, R., Suzuki, N.N., Horiuchi, M., Kohjima, M., Sumimoto, H., Inagaki, F. J. Biol. Chem. (2005) [Pubmed]
  20. The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex. Detjen, B.M., St Angelo, C., Katze, M.G., Krug, R.M. J. Virol. (1987) [Pubmed]
  21. Mutational analysis of the influenza virus A/Victoria/3/75 PA protein: studies of interaction with PB1 protein and identification of a dominant negative mutant. Zürcher, T., de la Luna, S., Sanz-Ezquerro, J.J., Nieto, A., Ortín, J. J. Gen. Virol. (1996) [Pubmed]
  22. Phylogenetic analysis of an H1N2 influenza A virus isolated from a pig in Korea. Brief Report. Jung, K., Chae, C. Arch. Virol. (2004) [Pubmed]
  23. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. Zamarin, D., Ortigoza, M.B., Palese, P. J. Virol. (2006) [Pubmed]
  24. Kinetic models for normal and impaired growth. Milani, S. Ann. Hum. Biol. (2000) [Pubmed]
 
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