Enhanceosome transcription factors preferentially dimerize with high mobility group proteins
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چکیده
منابع مشابه
CHARACTERIZATION OF HIGH MOBILITY GROUP NONHISTONE PROTEINS FROM DIFFERENTIATED NEUROPHILIC GRANULOCYTES
The quantitative changes of the high mobility group (HMG) nonhistone chromosomal proteins in nondividing, differentiated peritoneal exudate neutrophils were identified by their solubility, electrophoretic mobility on both SDS and acetic acid gels, densitometric traces and elution profile on CM-sephadex. The results indicated that in neutrophils, HMGl undergoes a considerable reduction (80%...
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Sox proteins are widely believed to team up with other transcription factors as partner proteins to perform their many essential functions during development. In this study, yeast two-hybrid screens identified transcription factors as a major group of interacting proteins for Sox8 and Sox10. Interacting transcription factors were very similar for these two group E Sox proteins and included prot...
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Viral particles at the late stages of SV40 morphogenesis were examined for the presence of HMG proteins 1 and 2, by an lmmunochemical method involving the transfer of proteins from polyacrylamide gels to nitrocellulose membranes. It was found that these proteins are present in SV40 provirions, in which histone HI is still associated with viral chromatin, but absent in mature SV40 virions. INTRO...
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Nucleosome core particles form well defined complexes with the nuclear nonhistone proteins HMG 14 or 17. The binding of HMG 14 or 17 to nucleosomes results in greater stability of the nucleosomal DNA as shown by circular dichroism and thermal denaturation. Under appropriate conditions the binding is cooperative, and cooperativity is ionic strength dependent. The specificity and cooperative tran...
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Four proteins have been extracted from purified chromatin of wheat embryos with 0.35 M NaCl. These proteins are soluble in 2% (w/v) trichloroacetic acid and thus meet the original operational requirements to be classified as "high-mobility group" (HMG) chromosomal proteins. The proteins have been characterized by one- and two-dimensional electrophoresis, amino acid analysis, and peptide mapping...
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ژورنال
عنوان ژورنال: BMC Systems Biology
سال: 2015
ISSN: 1752-0509
DOI: 10.1186/s12918-016-0258-3