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DETERMINATION OF SEQUENCES RESPONSIBLE FOR THE DIFFERENTIAL REGULATION OF MYC FUNCTION BY DELTA-MAX AND MAX
Tekijät: VÄSTRIK I, MÄKELÄ TP, KOSKINEN PJ, ALITALO K
Kustantaja: STOCKTON PRESS
Julkaisuvuosi: 1995
Journal: Oncogene
Tietokannassa oleva lehden nimi: ONCOGENE
Lehden akronyymi: ONCOGENE
Vuosikerta: 11
Numero: 3
Aloitussivu: 553
Lopetussivu: 560
Sivujen määrä: 8
ISSN: 0950-9232
Tiivistelmä
The DNA-binding, transcriptional activation and transforming activities of the Myc protein require dimerization with Max. Max can form also homodimers which are able to bind the same DNA sequence as Myc/Max heterodimers and suppress Myc-induced transcription and transformation. We have recently identified naturally occurring truncated form of Max, Delta Max, which in a rat embryo fibroblast enhances transformation by Myc and Ras, Like Max, this Delta Max protein contains a b-HLH-Zip domain, except that the end of the leucine zipper is replaced by five Delta Max-specific amino acid residues. Delta Max also lacks the C-terminal sequences of Max including a nuclear localisation signal. Here we have dissected the regions responsible for the specific effects of Max and Delta Max in Ras-Myc cotransformation of rat embryo fibroblasts, Our results indicate that the suppressive activity of Max requires C-terminal acidic and basic regions and an intact leucine zipper. Replacement of the end of the leucine zipper with the Delta Max-specific sequence is responsible for the enhancement of transformation by Delta Max. Surprisingly, Delta Max does not require the DNA-binding basic region for enhancement of transformation and has no effect on Myc-induced transcription activation from Myc/Max-binding site-containing promoter construct.
The DNA-binding, transcriptional activation and transforming activities of the Myc protein require dimerization with Max. Max can form also homodimers which are able to bind the same DNA sequence as Myc/Max heterodimers and suppress Myc-induced transcription and transformation. We have recently identified naturally occurring truncated form of Max, Delta Max, which in a rat embryo fibroblast enhances transformation by Myc and Ras, Like Max, this Delta Max protein contains a b-HLH-Zip domain, except that the end of the leucine zipper is replaced by five Delta Max-specific amino acid residues. Delta Max also lacks the C-terminal sequences of Max including a nuclear localisation signal. Here we have dissected the regions responsible for the specific effects of Max and Delta Max in Ras-Myc cotransformation of rat embryo fibroblasts, Our results indicate that the suppressive activity of Max requires C-terminal acidic and basic regions and an intact leucine zipper. Replacement of the end of the leucine zipper with the Delta Max-specific sequence is responsible for the enhancement of transformation by Delta Max. Surprisingly, Delta Max does not require the DNA-binding basic region for enhancement of transformation and has no effect on Myc-induced transcription activation from Myc/Max-binding site-containing promoter construct.
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