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- W3149712801 abstract "Using site-directed mutagenesis insertion or deletion,PHO2 gene was changed in strueture, the effect of these changes on its funetion was observed.The homeodomain of PHO2 protein has such structure as a-helix 2-turn-a-helix 3,which acts as DNA binding domain of transcriptional factor,A site-driected mutant of Ile123 to Pro123 in a-helix 3 or insertion of four amino acids(PDPD) into a-helix 2 can destroy the a-helix structure, and lead to inaotivation of PHO2.Deletion analysis of the Gln-rich region of the N-terminal had no effect on PHO2 functions,while deletion of the acidic region(residue 249～261) inactivate the PHO2 protein These results show that the acidic region may act as a transpriptional activation domain of PHO2. A short cluster of residues(241～258) shared 50% homology with residues 32 to 50 of the negative factor WHO80 and deletion of this ragion inactivated the PHO2 protein.So we concluded that this region might be an association domain of PHO2 and PHO4 protein." @default.
- W3149712801 created "2021-04-13" @default.
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- W3149712801 date "1995-01-01" @default.
- W3149712801 modified "2023-09-23" @default.
- W3149712801 title "Studies on the Function Domains of the Transcriptional Requlatory Factor PHO2 in Yeast Acid Phosphatase System" @default.
- W3149712801 hasPublicationYear "1995" @default.
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