scholarly journals Molecular Evaluation of Transformation‐Induced Methylation of the High Mobility Group A1 (HMGA1) Chromatin Binding Proteins

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Kendra Bufkin ◽  
Ronald Nelson ◽  
Jaiyue Deng ◽  
Takita Sumter
Keyword(s):  
Binding Proteins ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromatin Binding ◽  
Molecular Evaluation

scholarly journals High Mobility Group Protein-B1 Interacts with Sterol Regulatory Element-binding Proteins to Enhance Their DNA Binding

2005 ◽  
Vol 280 (30) ◽  
pp. 27523-27532 ◽  
Author(s):  
Yuho Najima ◽  
Naoya Yahagi ◽  
Yoshinori Takeuchi ◽  
Takashi Matsuzaka ◽  
Motohiro Sekiya ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Regulatory Element ◽  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Protein ◽  
Sterol Regulatory Element ◽  
Group Protein

scholarly journals The dynamics of HMG protein–chromatin interactions in living cellsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process.

2009 ◽  
Vol 87 (1) ◽  
pp. 127-137 ◽  
Author(s):  
Gabi Gerlitz ◽  
Robert Hock ◽  
Tetsuya Ueda ◽  
Michael Bustin
Keyword(s):  
Binding Sites ◽  
Binding Proteins ◽  
Peer Review Process ◽  
High Mobility ◽  
Structural Features ◽  
Chromatin Binding ◽  
Hmg Proteins ◽  
Chromatin Dynamics ◽  
Chromatin Interactions ◽  
Major Factors

The dynamic interaction between nuclear proteins and chromatin leads to the functional plasticity necessary to mount adequate responses to regulatory signals. Here, we review the factors regulating the chromatin interactions of the high mobility group proteins (HMGs), an abundant and ubiquitous superfamily of chromatin-binding proteins in living cells. HMGs are highly mobile and interact with the chromatin fiber in a highly dynamic fashion, as part of a protein network. The major factors that affect the binding of HMGs to chromatin are operative at the level of the single nucleosome. These factors include structural features of the HMGs, competition with other chromatin-binding proteins for nucleosome binding sites, complex formation with protein partners, and post-translational modifications in the protein or in the chromatin-binding sites. The versatile modulation of the interaction between HMG proteins and chromatin plays a role in processes that establish the cellular phenotype.

scholarly journals Hepatic Nuclear Factor 3 and High Mobility Group I/Y Proteins Bind the Insulin Response Element of the Insulin-Like Growth Factor-Binding Protein-1 Promoter*

Endocrinology ◽  
1997 ◽  
Vol 138 (10) ◽  
pp. 4291-4300 ◽  
Author(s):  
Susanne V. Allander ◽  
Susan K. Durham ◽  
Ann O. Scheimann ◽  
Richard M. Wasserman ◽  
Adisak Suwanichkul ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hormonal Regulation ◽  
Binding Proteins ◽  
Insulin Response ◽  
High Mobility ◽  
High Mobility Group ◽  
Nuclear Factor ◽  
Response Element ◽  
Factor Binding ◽  
Group I

Abstract The insulin response element (IRE) of the human insulin-like growth factor-binding protein-1 (IGFBP-1) promoter contains a palindrome of the T(A/G)TTT sequence crucial to hormonal regulation of many genes. In initial studies of how this IRE participates in hormonal regulation, the electromobility shift assay was used under a variety of conditions to identify IRE-binding proteins. An exhaustive search identified five proteins that specifically bind this IRE; purified proteins were used to show that all five are related to either the high mobility group I/Y (HMGI/Y) or hepatic nuclear factor 3 (HNF3) protein families. Further studies used purified HNF3 and HMGI proteins to show: 1) each protects the IGFBP-1 IRE from deoxyribonuclease I (DNaseI) digestion; and 2) HNF3 but not HMGI/Y binds to the related phosphoenolpyruvate carboxykinase and Apo CIII IREs. A series of IRE mutants with variable responsiveness to insulin were used to show that the presence of a TGTTT sequence in the mutants did parallel, but HMGI/Y and HNF3 binding to the mutants did not parallel, the ability of the mutants to confer the inhibitory effect of insulin. In contrast, HNF3 binding to these IRE mutants roughly correlates with response of the mutants to glucocorticoids. The way by which HNF3 and/or other as yet unidentified IRE-binding proteins confer insulin inhibition to IGFBP-1 transcription and the role of HMGI/Y in IRE function have yet to be established.

scholarly journals Network of Dynamic Interactions between Histone H1 and High-Mobility-Group Proteins in Chromatin

2004 ◽  
Vol 24 (10) ◽  
pp. 4321-4328 ◽  
Author(s):  
Frédéric Catez ◽  
Huan Yang ◽  
Kevin J. Tracey ◽  
Raymond Reeves ◽  
Tom Misteli ◽  
...  
Keyword(s):  
Binding Sites ◽  
High Mobility ◽  
Histone H1 ◽  
Chromatin Fiber ◽  
High Mobility Group ◽  
Chromatin Binding ◽  
Hmg Proteins ◽  
Dynamic Interactions ◽  
Regulate Gene Expression ◽  
Regulatory Factors

ABSTRACT Histone H1 and the high-mobility group (HMG) proteins are chromatin binding proteins that regulate gene expression by modulating the compactness of the chromatin fiber and affecting the ability of regulatory factors to access their nucleosomal targets. Histone H1 stabilizes the higher-order chromatin structure and decreases nucleosomal access, while the HMG proteins decrease the compactness of the chromatin fiber and enhance the accessibility of chromatin targets to regulatory factors. Here we show that in living cells, each of the three families of HMG proteins weakens the binding of H1 to nucleosomes by dynamically competing for chromatin binding sites. The HMG families weaken H1 binding synergistically and do not compete among each other, suggesting that they affect distinct H1 binding sites. We suggest that a network of dynamic and competitive interactions involving HMG proteins and H1, and perhaps other structural proteins, constantly modulates nucleosome accessibility and the local structure of the chromatin fiber.

Sign in / Sign up

Export Citation Format

Share Document