Pho4

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Phosphate system positive regulatory protein '''Pho4''' is a transcriptional activator which regulates the expression of phosphatase under conditions of phosphate starvation<ref>PMID:2220078</ref>. For details see [[Pho4 bHLH Protein]].
Phosphate system positive regulatory protein '''Pho4''' is a transcriptional activator which regulates the expression of phosphatase under conditions of phosphate starvation<ref>PMID:2220078</ref>. For details see [[Pho4 bHLH Protein]].
*<scene name='72/725407/Cv/2'>Yeast Pho4 DNA-binding domain interactions with DNA</scene>.
*<scene name='72/725407/Cv/2'>Yeast Pho4 DNA-binding domain interactions with DNA</scene>.
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Its structure is a basic basic helix-loop-helix (bHLH) [1]
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Its structure is a basic basic helix-loop-helix (bHLH)<ref>PMID:2220078</ref>
The pho4 protein takes part in transcription of several yeast genes related to phosphate metabolism:
The pho4 protein takes part in transcription of several yeast genes related to phosphate metabolism:
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PH05- encoding repressible acid phosphatase [2]
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PH05- encoding repressible acid phosphatase
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PH08-encoding alkaline phosphatase [2]
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PH08-encoding alkaline phosphatase<ref>PMID:2671650</ref>
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PH081-a regulatory gene [3]
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PH081-a regulatory gene<ref>PMID:2671650</ref>
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PH084- phosphate permease gene [4]
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PH084- phosphate permease gene<ref>PMID:3902805</ref>
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==sturcture==
==sturcture==
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The structure of the Pho4 protein is a basic Helix-loop-helix(bHLH) , The linker sequence between Helix1(H1) and Helix2(H2) contains several residues: Asn, Glu, Pro and Ser[6]. The DNA binding site is a homodimer and two monomers in a left‐handed four‐helix bundle fold (identical to bHLH/Zip and bHLH proteins fold) [7].
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The structure of the Pho4 protein is a basic Helix-loop-helix(bHLH) , The linker sequence between Helix1(H1) and Helix2(H2) contains several residues: Asn, Glu, Pro and Ser<ref>PMID: 3775366</ref> . The DNA binding site is a homodimer and two monomers in a left‐handed four‐helix bundle fold (identical to bHLH/Zip and bHLH proteins fold) .
[[loop structure]]
[[loop structure]]
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Pho4 loops (conserved structure?) are long but compact and forms a short alpha-helical structure [5]. The PHO4 loop contains a Trp residue that faces the aromatic rings of Tyr52 and His55 of helix H2, and Pro28 of H2 and H1.an aromatic cluster forms a cap structure is observed.
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Pho4 loops (conserved structure?) are long but compact and forms a short alpha-helical structure <ref>PMID:1170095</ref>. The PHO4 loop contains a Trp residue that faces the aromatic rings of Tyr52 and His55 of helix H2, and Pro28 of H2 and H1.an aromatic cluster forms a cap structure is observed.<ref>PMID: 9303313</ref>

Revision as of 12:35, 19 March 2018

Yeast Pho4 DNA-binding domain complex with DNA (PDB code 1a0a)

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sturcture

The structure of the Pho4 protein is a basic Helix-loop-helix(bHLH) , The linker sequence between Helix1(H1) and Helix2(H2) contains several residues: Asn, Glu, Pro and Ser[6] . The DNA binding site is a homodimer and two monomers in a left‐handed four‐helix bundle fold (identical to bHLH/Zip and bHLH proteins fold) .

loop structure Pho4 loops (conserved structure?) are long but compact and forms a short alpha-helical structure [7]. The PHO4 loop contains a Trp residue that faces the aromatic rings of Tyr52 and His55 of helix H2, and Pro28 of H2 and H1.an aromatic cluster forms a cap structure is observed.[8]


3D Structures of lactoferrin

Updated on 19-March-2018

1a0a – yPho4 DNA-binding domain + DNA - yeast
3w3x – yPho4 peptide + importin subunit b-3

References

  1. ↑ Berben G, Legrain M, Gilliquet V, Hilger F. The yeast regulatory gene PHO4 encodes a helix-loop-helix motif. Yeast. 1990 Sep-Oct;6(5):451-4. PMID:2220078 doi:http://dx.doi.org/10.1002/yea.320060510
  2. ↑ Berben G, Legrain M, Gilliquet V, Hilger F. The yeast regulatory gene PHO4 encodes a helix-loop-helix motif. Yeast. 1990 Sep-Oct;6(5):451-4. PMID:2220078 doi:http://dx.doi.org/10.1002/yea.320060510
  3. ↑ Yoshida K, Ogawa N, Oshima Y. Function of the PHO regulatory genes for repressible acid phosphatase synthesis in Saccharomyces cerevisiae. Mol Gen Genet. 1989 May;217(1):40-6. PMID:2671650
  4. ↑ Yoshida K, Ogawa N, Oshima Y. Function of the PHO regulatory genes for repressible acid phosphatase synthesis in Saccharomyces cerevisiae. Mol Gen Genet. 1989 May;217(1):40-6. PMID:2671650
  5. ↑ Tamai Y, Toh-e A, Oshima Y. Regulation of inorganic phosphate transport systems in Saccharomyces cerevisiae. J Bacteriol. 1985 Nov;164(2):964-8. PMID:3902805
  6. ↑ Leszczynski JF, Rose GD. Loops in globular proteins: a novel category of secondary structure. Science. 1986 Nov 14;234(4778):849-55. PMID:3775366
  7. ↑ Schmeckpeper BJ, Adams JM, Harris AW. Detection of a possible precursor of immunoglobulin light chain in MOPC 41 A plasmacytoma cells. FEBS Lett. 1975 Apr 15;53(1):95-8. PMID:1170095
  8. ↑ Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T. Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition. EMBO J. 1997 Aug 1;16(15):4689-97. PMID:9303313 doi:10.1093/emboj/16.15.4689

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Michal Harel, Inbar Yaffe, Alexander Berchansky, Joel L. Sussman

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