Gene-regulatory properties of Myc helix-loop-helix/leucine zipper mutants: Max-dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity

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Gene-regulatory properties of Myc helix-loop-helix/leucine zipper mutants : Max-dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity. / Crouch, D H; Fisher, F; Clark, W; Jayaraman, P S; Goding, C R; Gillespie, D A.

In: Oncogene, Vol. 8, No. 7, 07.1993, p. 1849-55.

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@article{a75127c242a447ae8756ee8dc31226f3,
title = "Gene-regulatory properties of Myc helix-loop-helix/leucine zipper mutants: Max-dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity",
abstract = "Max is a basic helix-loop-helix/leucine zipper (bHLH/LZ) protein that forms sequence-specific DNA-binding complexes with the c-Myc oncoprotein (Myc). Using Saccharomyces cerevisiae, we have shown that the Max bHLH/LZ domain enables Myc to activate transcription through CACGTG and CACATG sequences in vivo, and that the number and context of such sites determines the level of activation. In addition, we have used yeast to investigate the role of the Myc helix-loop-helix (HLH) and leucine zipper (LZ) motifs in mediating Max-dependent DNA-binding and transcriptional activation in vivo using HLH/LZ mutants generated by site-directed mutagenesis. The results show that, while both motifs are essential for Myc to activate transcription, helix 2 of the HLH together with the contiguous LZ suffice to mediate complex formation with Max, whilst helix 1 is essential for sequence-specific DNA binding of Myc-Max complexes. Furthermore, the ability of Myc HLH/LZ mutants to bind DNA and activate transcription in collaboration with Max correlates closely with their neoplastic transforming activity in higher eukaryotic cells.",
keywords = "Base Sequence, Basic-Leucine Zipper Transcription Factors, Cell Transformation, Neoplastic, DNA, DNA-Binding Proteins, Leucine Zippers, Molecular Sequence Data, Mutation, Protein Structure, Secondary, Proto-Oncogene Proteins c-myc, Saccharomyces cerevisiae, Transcription Factors, Transcriptional Activation",
author = "Crouch, {D H} and F Fisher and W Clark and Jayaraman, {P S} and Goding, {C R} and Gillespie, {D A}",
year = "1993",
month = jul,
language = "English",
volume = "8",
pages = "1849--55",
journal = "Oncogene",
issn = "0950-9232",
publisher = "Nature Publishing Group",
number = "7",

}

RIS

TY - JOUR

T1 - Gene-regulatory properties of Myc helix-loop-helix/leucine zipper mutants

T2 - Max-dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity

AU - Crouch, D H

AU - Fisher, F

AU - Clark, W

AU - Jayaraman, P S

AU - Goding, C R

AU - Gillespie, D A

PY - 1993/7

Y1 - 1993/7

N2 - Max is a basic helix-loop-helix/leucine zipper (bHLH/LZ) protein that forms sequence-specific DNA-binding complexes with the c-Myc oncoprotein (Myc). Using Saccharomyces cerevisiae, we have shown that the Max bHLH/LZ domain enables Myc to activate transcription through CACGTG and CACATG sequences in vivo, and that the number and context of such sites determines the level of activation. In addition, we have used yeast to investigate the role of the Myc helix-loop-helix (HLH) and leucine zipper (LZ) motifs in mediating Max-dependent DNA-binding and transcriptional activation in vivo using HLH/LZ mutants generated by site-directed mutagenesis. The results show that, while both motifs are essential for Myc to activate transcription, helix 2 of the HLH together with the contiguous LZ suffice to mediate complex formation with Max, whilst helix 1 is essential for sequence-specific DNA binding of Myc-Max complexes. Furthermore, the ability of Myc HLH/LZ mutants to bind DNA and activate transcription in collaboration with Max correlates closely with their neoplastic transforming activity in higher eukaryotic cells.

AB - Max is a basic helix-loop-helix/leucine zipper (bHLH/LZ) protein that forms sequence-specific DNA-binding complexes with the c-Myc oncoprotein (Myc). Using Saccharomyces cerevisiae, we have shown that the Max bHLH/LZ domain enables Myc to activate transcription through CACGTG and CACATG sequences in vivo, and that the number and context of such sites determines the level of activation. In addition, we have used yeast to investigate the role of the Myc helix-loop-helix (HLH) and leucine zipper (LZ) motifs in mediating Max-dependent DNA-binding and transcriptional activation in vivo using HLH/LZ mutants generated by site-directed mutagenesis. The results show that, while both motifs are essential for Myc to activate transcription, helix 2 of the HLH together with the contiguous LZ suffice to mediate complex formation with Max, whilst helix 1 is essential for sequence-specific DNA binding of Myc-Max complexes. Furthermore, the ability of Myc HLH/LZ mutants to bind DNA and activate transcription in collaboration with Max correlates closely with their neoplastic transforming activity in higher eukaryotic cells.

KW - Base Sequence

KW - Basic-Leucine Zipper Transcription Factors

KW - Cell Transformation, Neoplastic

KW - DNA

KW - DNA-Binding Proteins

KW - Leucine Zippers

KW - Molecular Sequence Data

KW - Mutation

KW - Protein Structure, Secondary

KW - Proto-Oncogene Proteins c-myc

KW - Saccharomyces cerevisiae

KW - Transcription Factors

KW - Transcriptional Activation

M3 - Article

C2 - 8510929

VL - 8

SP - 1849

EP - 1855

JO - Oncogene

JF - Oncogene

SN - 0950-9232

IS - 7

ER -