Pho4: Difference between revisions
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== Function == | == Function == | ||
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 in Saccharomyces cerevisiae <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>. | ||
Its structure is a basic basic helix-loop-helix (bHLH)<ref>PMID:2220078</ref> | 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: | ||
[[PH05]] encoding repressible acid phosphatase | [[PH05]] encoding repressible acid phosphatase, | ||
[[PH08]] encoding alkaline phosphatase<ref>PMID:2671650</ref> | [[PH08]] encoding alkaline phosphatase<ref>PMID:2671650</ref> | ||
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[[PH084]] phosphate permease gene<ref>PMID:3902805</ref> | [[PH084]] phosphate permease gene<ref>PMID:3902805</ref> | ||
other than that, the Pho4 protein seems to contain a coding region for non translated mitochondrial proteins<ref>PMID:2183025</ref> | |||
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==sturcture== | ==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<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) . | 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 | ||
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> | 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> | ||
*DNA binding | |||
As The Pho4 binding region binds specifically to CACGTG sequence by a specific subset of the basic region of the bHLH motif<ref>PMID:1861859</ref> | |||
Revision as of 14:21, 19 March 2018
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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[1]. 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 [2]. 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.[3]
- DNA binding
As The Pho4 binding region binds specifically to CACGTG sequence by a specific subset of the basic region of the bHLH motif[4]
3D Structures of lactoferrin
Updated on 19-March-2018
Pho4 bHLH Protein – yPho4 DNA-binding domain + DNA - yeast
PH05 – yPho4 peptide + importin subunit b-3
References
- ↑ Leszczynski JF, Rose GD. Loops in globular proteins: a novel category of secondary structure. Science. 1986 Nov 14;234(4778):849-55. PMID:3775366
- ↑ 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
- ↑ 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
- ↑ Fisher F, Jayaraman PS, Goding CR. C-myc and the yeast transcription factor PHO4 share a common CACGTG-binding motif. Oncogene. 1991 Jul;6(7):1099-104. PMID:1861859
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Inbar Yaffe, Michal Harel, Alexander Berchansky, Joel L. Sussman
