scholarly journals Two new low-molecular-weight acidic proteins from calf thymus nuclei that resemble HMG (high-mobility-group) proteins 14 and 17

1982 ◽  
Vol 207 (3) ◽  
pp. 519-527 ◽  
Author(s):  
P D Cary
Keyword(s):  
Molecular Weight ◽  
Tertiary Structure ◽  
High Mobility ◽  
High Mobility Group ◽  
Proton Nuclear Magnetic Resonance ◽  
High Mobility Group Proteins ◽  
Calf Thymus ◽  
Hydrophobic Amino Acids ◽  
Thymus Nucleus ◽  
Acidic Proteins

Two new, closely similar, acidic proteins were extracted and purified from calf thymus and designated AP-X and AP-Y (acidic proteins X and Y). They contain about 33% acidic residues, mostly non-amidated, and 20% lysine, but no arginine, tyrosine, histidine or tryptophan. There is a single phenylalanine residue in a molecular weight of approx. 5000. Circular dichroism and proton nuclear magnetic resonance show that they do not take up secondary or tertiary structure in free solution, as expected from the low content of hydrophobic amino acids. They appear structurally related to the high-mobility-group proteins HMG 14 and 17. Controlled extraction experiments indicate that proteins AP-X and AP-Y are at least partially located in the calf thymus nucleus.

scholarly journals HMG (high-mobility-group)-14/17-like proteins in calf thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins

1983 ◽  
Vol 215 (3) ◽  
pp. 643-649 ◽  
Author(s):  
E Cooper ◽  
S W Spaulding
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
High Mobility Group ◽  
Group 14 ◽  
Sephadex Column ◽  
High Mobility Group Proteins ◽  
Electrophoretic Mobilities ◽  
Calf Thymus ◽  
Thymus Tissue

Two-dimensional polyacrylamide-gel electrophoresis of acid extracts of thyroid and thymus tissue, and of thyroid nuclei, revealed the presence of three HClO4-soluble nuclear proteins, PS.1, PS.2 and PS.3, whose electrophoretic mobilities closely resembled those of HMG (high-mobility-group) proteins 14 and 17. PS.1 co-migrated with HMG 14 on CM-Sephadex column chromatography. Like HMG 14, PS.2 and PS.3 were phosphorylated in calf thyroid slices; 32P-labelling of PS.3 was stimulated by thyrotropin. Thyrotropin also induced a rapid increase in the labelling of A5, an HMG-14/17-like protein found in whole calf thyroid and thymus tissue, but not in thyroid nuclei.

scholarly journals Isolation of a high-molecular-weight high-mobility-group-type non-histone protein from hen oviduct

1978 ◽  
Vol 176 (3) ◽  
pp. 1003-1006 ◽  
Author(s):  
C S Teng ◽  
K Gallagher ◽  
C T Teng
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
High Mobility ◽  
High Mobility Group ◽  
Histone Protein ◽  
Basic Amino Acids ◽  
Group Type ◽  
High Mobility Group Proteins ◽  
Organ Specific

An organ-specific non-histone protein, with a mol.wt. of 95,000, was isolated from hen oviduct. This protein consists of approximately equal amounts of acidic and basic amino acids and has an isolectric point of 7.4. On the basis of its known characteristics, this protein is similar to the high-mobility-group proteins observed in other tissues.

Structural Studies on Two High-Mobility-Group Proteins from Calf Thymus, HMG-14 and HMG-20 (Ubiquitin), and Their Interaction with DNA

2005 ◽  
Vol 112 (3) ◽  
pp. 577-580 ◽  
Author(s):  
Peter D. CARY ◽  
Deborah S. KING ◽  
Colyn CRANE-ROBINSON ◽  
E. Morton BRADBURY ◽  
Azra RABBANI ◽  
...  
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Structural Studies ◽  
High Mobility Group Proteins ◽  
Calf Thymus

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
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