Differential expression of the chromosomal high mobility group proteins 14 and 17 during the onset of differentiation in mammalian osteoblasts and promyelocytic leukemia cells

1993 ◽  
Vol 51 (4) ◽  
pp. 479-487 ◽  
Author(s):  
Abdul Rauf Shakoori ◽  
Thomas A. Owen ◽  
Victoria Shalhoub ◽  
Janet L. Stein ◽  
Michael Bustin ◽  
...  
Keyword(s):  
Differential Expression ◽  
High Mobility ◽  
Promyelocytic Leukemia ◽  
High Mobility Group ◽  
Leukemia Cells ◽  
High Mobility Group Proteins

scholarly journals Positioning of nucleosomes containing γ-H2AX precedes active DNA demethylation and transcription initiation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Stephanie Dobersch ◽  
Karla Rubio ◽  
Indrabahadur Singh ◽  
Stefan Günther ◽  
Johannes Graumann ◽  
...  
Keyword(s):  
Transcription Initiation ◽  
High Mobility ◽  
Dna Demethylation ◽  
High Mobility Group ◽  
Regulation Of Transcription ◽  
Dna Breaks ◽  
Transcriptional Initiation ◽  
High Mobility Group Proteins ◽  
Active Dna Demethylation ◽  
Repair Mechanisms

AbstractIn addition to nucleosomes, chromatin contains non-histone chromatin-associated proteins, of which the high-mobility group proteins are the most abundant. Chromatin-mediated regulation of transcription involves DNA methylation and histone modifications. However, the order of events and the precise function of high-mobility group proteins during transcription initiation remain unclear. Here we show that high-mobility group AT-hook 2 protein (HMGA2) induces DNA nicks at the transcription start site, which are required by the histone chaperone FACT complex to incorporate nucleosomes containing the histone variant H2A.X. Further, phosphorylation of H2A.X at S139 (γ-H2AX) is required for repair-mediated DNA demethylation and transcription activation. The relevance of these findings is demonstrated within the context of TGFB1 signaling and idiopathic pulmonary fibrosis, suggesting therapies against this lethal disease. Our data support the concept that chromatin opening during transcriptional initiation involves intermediates with DNA breaks that subsequently require DNA repair mechanisms to ensure genome integrity.

scholarly journals Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry

2008 ◽  
Vol 9 (1) ◽  
pp. 170-179 ◽  
Author(s):  
Donna R Louie ◽  
Kristen K. Gloor ◽  
Scott C. Galasinski ◽  
Katheryn A. Resing ◽  
Natalie G. Ahn
Keyword(s):  
Mass Spectrometry ◽  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Proteins

High mobility group proteins: abundance, turnover and relationship to transcriptionally active chromatin

Biochemistry ◽  
1983 ◽  
Vol 22 (21) ◽  
pp. 5008-5015 ◽  
Author(s):  
Ronald L. Seale ◽  
Anthony T. Annunziato ◽  
Richard D. Smith
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Active Chromatin ◽  
High Mobility Group Proteins

scholarly journals Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues.

1984 ◽  
Vol 99 (2) ◽  
pp. 648-654 ◽  
Author(s):  
L Kuehl ◽  
B Salmond ◽  
L Tran
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Rat Tissues ◽  
Two Dimensional ◽  
Hmg Proteins ◽  
High Mobility Group Proteins

Nuclear and cytoplasmic fractions were isolated from various tissues of the rat by a nonaqueous technique. The high-mobility-group (HMG) proteins were extracted from these fractions with acid and separated by one- and two-dimensional PAGE. The concentrations of high-mobility-group proteins HMG1, HMG2, and HMG17 in the nucleus and cytoplasm were then estimated from the staining intensities of the electrophoretic bands. The cytoplasmic concentrations of these proteins were very low--usually less than 1/30 of those present in the corresponding nuclear fractions. For the tissues studied (liver, kidney, heart, and lung), the concentrations of HMG proteins in the nucleus did not differ significantly from one tissue to another. Averaged over the four tissues investigated, there were 0.28 molecule of HMG1, 0.18 molecule of HMG2, and 0.46 molecule of HMG17 per nucleosome. These values are considerably higher than those that have been reported previously.

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