Pho4 bHLH Protein: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
|||
(5 intermediate revisions by one other user not shown) | |||
Line 18: | Line 18: | ||
---- | ---- | ||
PHO4 transcription factor is a basic helix loop helix structure with 312 amino acid residues with 4 functional domains commonly found in S. cerevisiae( | PHO4 transcription factor is a basic helix loop helix structure with 312 amino acid residues with 4 functional domains commonly found in S. cerevisiae(6). The amount of enviornmental inorganic phosphate regulates the activity of PHO4 binding (5). | ||
PHO4 is a regulatory protein active during phosphorylation. When phosphates are abundant PHO4 becomes phosphorylated by cyclin PHO80 and cyclin-dependent kinase PHO85, which causes PHO4 to become transported from nucleous to cytoplasm ( | PHO4 is a regulatory protein active during phosphorylation. When phosphates are abundant PHO4 becomes phosphorylated by cyclin PHO80 and cyclin-dependent kinase PHO85, which causes PHO4 to become transported from nucleous to cytoplasm (5). | ||
When there is limited amount of phosphate PHO4 is dephosphorylated and transported into the nucleous which activates the gene for transcription ( | When there is limited amount of phosphate PHO4 is dephosphorylated and transported into the nucleous which activates the gene for transcription (5). The particular genes at which PHO4 activaes are PHO5, PHO81 and PHO84(2). A cooperative interaction between transcription factor PHO2 and PHO4 typically occurs in order to activate the PHO5 gene(5). | ||
Base flanking of PHO4 was compared to other bHLH structures such as MyoD, MAX, USF, E47 and CPF1( | Base flanking of PHO4 was compared to other bHLH structures such as MyoD, MAX, USF, E47 and CPF1(6). The binding angle degree of each structure may be a determining factor for specific dimer formation (6) | ||
Other molecules such as nucleosomes and Cbf1 can cause PHO4 to not bind to promoter due to competition for the promoter site CACGTG ( | Other molecules such as nucleosomes and Cbf1 can cause PHO4 to not bind to promoter due to competition for the promoter site CACGTG (6). | ||
In the PHO5 gene,Due to PHO4 binding disrupting nucleosome binding structure this can cause chromatin reorganization of the PHO5 and murine mammary tumor virus(or mouse mammary tumor virus) promoters( | In the PHO5 gene,Due to PHO4 binding disrupting nucleosome binding structure this can cause chromatin reorganization of the PHO5 and murine mammary tumor virus(or mouse mammary tumor virus) promoters(7). In order for MMTV to activate nucleosomes must be present, PHO4 can act as a way to inhibit the formation of nucleosome binding within this virus (7). | ||
MMTV is a retrovirus which is transmitted by infected mother to offspring via breast milk due to extra choromsome ( | MMTV is a retrovirus which is transmitted by infected mother to offspring via breast milk due to extra choromsome (8). | ||
The virus is typically integrated within the host DNA and is generally transported into the host via the gastrointestinal tract infecting the immune system( | The virus is typically integrated within the host DNA and is generally transported into the host via the gastrointestinal tract infecting the immune system(9). | ||
Dendritic cells are the first infected cells in the MMTV virus which then are transmitted to other cell types( | Dendritic cells are the first infected cells in the MMTV virus which then are transmitted to other cell types(9). When the virus infects dendritic cells they then become more mature and start migrating in response to chemokine macrophage inflammatory protein 3β(9). | ||
Line 67: | Line 67: | ||
'''Predicted functional partners of Pho4''' | '''Predicted functional partners of Pho4''' | ||
•PH0 80 | |||
•PHO85 | |||
•PHO2 | |||
•PHO81 | |||
•MSN5 | |||
•PSE1 | |||
•SUA7 | |||
•SPT 15 | |||
•PHO4 | |||
•IN04 | |||
Sequence comparison to large number of mammalian and Drophilia BHLH proteins reveales similarity in the bHLH region. | Sequence comparison to large number of mammalian and Drophilia BHLH proteins reveales similarity in the bHLH region. | ||
Line 95: | Line 95: | ||
[[Category: Transcription-dna complex]] | [[Category: Transcription-dna complex]] | ||
1. Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T."Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Nat. Genet. 10:261-268(1995) [PubMed: 7670463] | |||
2. Legrain M., de Wilde M., Hilger F."Isolation, physical characterization and expression analysis of the Saccharomyces cerevisiae positive regulatory gene PHO4." Nucleic Acids Res. 14:3059-3073(1986) [PubMed: 3008105] | |||
3. Ogawa Nobuo, Oshima Yasuji (May 1990). ‘’Functional Domains of a Positive Regulatory Protein, PHO4, for Transcriptional Control of the Phosphatase Regulon in Saccharomyces cerevisiae. Molecular and Cellular Biology. 10 (5): 2224-2236. PMC 360570. PMID 2183025. | |||
4. Zhou Xu and O’Shea Erin K. (June 2011). ‘’ Integrated approaches reveal determinants of genome-wide binding and function of the transcription factor Pho4. Molecular Cell. 42 (6): 826-836. PMC 3127084. NIHM 305276. | |||
5. Zhou X, O’Shea E (2011) Integrated approaches reveal determinants of genome-wide binding and function of the transcription factor PHO4. Mol Cell 42(6): 826-836 | |||
6. Shimizu T, Toumoto A et. al. (1997) Crystal Structure of PHO4 bHLH domain-DNA complex: flanking base recognition. The EMBO Journal 16(15): 4689-4697 | |||
7. Bergh F, Flinn E M. (2000) Comparision of Nucleosome Remodeling by Yeast Transcription Factor PHO4 and the Glucocorticoid Recptor. The Journal of Biological Chemistry 275(12): 9035-9042 | |||
8. Bittner, J. J. (1936). Some Possible Effects of Nursing on the Mammary Gland Tumor Incidence in Mice. Science 84 (2172): 162–162 | |||
9. Courreges C M, et. al. Critical Role of Dendritic Cells in Mouse Mammary Tumor Virus In Vivo Infection. Journal of Virology 81(8) 3769-3777 |