A cellular factor stimulates the DNA-binding activity of MyoD and E47

Mathew (Matt) Thayer, Harold Weintraub

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

We show that mixing purified MyoD and E47 proteins results in heterodimers that fail to bind DNA, even though MyoD and E47 homodimers can bind DNA efficiently. Addition of cell extracts or a specific fraction from a cell extract enables the heterodimer to bind DNA, but components in this fraction fail to enter the DNA complex. The activity is sensitive to heat and protease and is not ATP-dependent. The activity functions on E47 and MyoD homodimers and can stimulate DNA binding of the basic-helix-loop-helix region of MyoD. The effectiveness of the activity, for MyoD homodimers, depends on the exact DNA sequence of the binding site. Our results suggest that specific factors in the cell might control the DNA-binding properties of helix-loop-helix proteins.

Original languageEnglish (US)
Pages (from-to)6483-6487
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number14
StatePublished - Jul 15 1993

Fingerprint

DNA
Cell Extracts
MyoD Protein
Peptide Hydrolases
Hot Temperature
Adenosine Triphosphate
Binding Sites
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

A cellular factor stimulates the DNA-binding activity of MyoD and E47. / Thayer, Mathew (Matt); Weintraub, Harold.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, No. 14, 15.07.1993, p. 6483-6487.

Research output: Contribution to journalArticle

@article{464b97c5e1d040b392ea3f475542f50a,
title = "A cellular factor stimulates the DNA-binding activity of MyoD and E47",
abstract = "We show that mixing purified MyoD and E47 proteins results in heterodimers that fail to bind DNA, even though MyoD and E47 homodimers can bind DNA efficiently. Addition of cell extracts or a specific fraction from a cell extract enables the heterodimer to bind DNA, but components in this fraction fail to enter the DNA complex. The activity is sensitive to heat and protease and is not ATP-dependent. The activity functions on E47 and MyoD homodimers and can stimulate DNA binding of the basic-helix-loop-helix region of MyoD. The effectiveness of the activity, for MyoD homodimers, depends on the exact DNA sequence of the binding site. Our results suggest that specific factors in the cell might control the DNA-binding properties of helix-loop-helix proteins.",
author = "Thayer, {Mathew (Matt)} and Harold Weintraub",
year = "1993",
month = "7",
day = "15",
language = "English (US)",
volume = "90",
pages = "6483--6487",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "14",

}

TY - JOUR

T1 - A cellular factor stimulates the DNA-binding activity of MyoD and E47

AU - Thayer, Mathew (Matt)

AU - Weintraub, Harold

PY - 1993/7/15

Y1 - 1993/7/15

N2 - We show that mixing purified MyoD and E47 proteins results in heterodimers that fail to bind DNA, even though MyoD and E47 homodimers can bind DNA efficiently. Addition of cell extracts or a specific fraction from a cell extract enables the heterodimer to bind DNA, but components in this fraction fail to enter the DNA complex. The activity is sensitive to heat and protease and is not ATP-dependent. The activity functions on E47 and MyoD homodimers and can stimulate DNA binding of the basic-helix-loop-helix region of MyoD. The effectiveness of the activity, for MyoD homodimers, depends on the exact DNA sequence of the binding site. Our results suggest that specific factors in the cell might control the DNA-binding properties of helix-loop-helix proteins.

AB - We show that mixing purified MyoD and E47 proteins results in heterodimers that fail to bind DNA, even though MyoD and E47 homodimers can bind DNA efficiently. Addition of cell extracts or a specific fraction from a cell extract enables the heterodimer to bind DNA, but components in this fraction fail to enter the DNA complex. The activity is sensitive to heat and protease and is not ATP-dependent. The activity functions on E47 and MyoD homodimers and can stimulate DNA binding of the basic-helix-loop-helix region of MyoD. The effectiveness of the activity, for MyoD homodimers, depends on the exact DNA sequence of the binding site. Our results suggest that specific factors in the cell might control the DNA-binding properties of helix-loop-helix proteins.

UR - http://www.scopus.com/inward/record.url?scp=0027184480&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027184480&partnerID=8YFLogxK

M3 - Article

C2 - 8393567

AN - SCOPUS:0027184480

VL - 90

SP - 6483

EP - 6487

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 14

ER -