The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes-Reference-Cited by-同舟云学术

The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes

Published:1993-04-01 Issue:13 Volume:32 Page:3238-3248
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sheflin Lowell G.,Fucile Nancy W.,Spaulding Stephen W.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00064a005

Reference87 articles.

1. Acetylated HMG1 protein interacts specifically with homologous DNA polymerase alpha in vitro

2. Circular dichroism and DNA secondary structure

3. Specific Recognition of Cruciform DNA by Nuclear Protein HMG1

4. The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins.

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