Multimeric complexes of differentiation-inducing protein bound to DNA.

Abstract:

:Myeloid hematopoietic precursor cells are induced to differentiate by the macrophage and granulocyte differentiation-inducing protein MGI-2 (DF). This differentiation-inducing protein bound to double-stranded but not to single-stranded mammalian DNA. The bound MGI-2 was not eluted by high salt, but was eluted by sodium dodecyl sulfate (SDS). MGI-2 also bound to double-stranded E. coli DNA, but with this DNA the bound MGI-2 was eluted by high salt. This indicated a difference in the binding affinities of MGI-2 to mammalian and E. coli DNA. MGI-2 bound to DNA was examined by electron microscopy. The results indicate that MGI-2 formed a multimeric complex with double-stranded DNA and that the size of the complex was correlated with the strength of protein binding to the DNA. The multimeric complex bound to DNA was disrupted by deoxyribonuclease. The data indicated that binding of this differentiation-inducing protein to DNA involves the formation of a multimeric complex in which the monomers are held together by DNA. It is suggested that the formation of such multimeric complexes of MGI-2 and DNA may allow activation of the multiple pathways of gene expression that is required for differentiation.

journal_name

Eur J Cell Biol

authors

Weisinger G,Korn AP,Sachs L

subject

Has Abstract

pub_date

1985-05-01 00:00:00

pages

196-202

eissn

0171-9335

issn

1618-1298

journal_volume

37

pub_type

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