scholarly journals Fractionation by high-performance liquid chromatography of the low-molecular-mass high-mobility-group (HMG) chromosomal proteins present in proliferating rat cells and an investigation of the HMG proteins present in virus transformed cells

1985 ◽  
Vol 149 (1) ◽  
pp. 47-51 ◽  
Author(s):  
Graham H. GOODWIN ◽  
Peter N. COCKERILL ◽  
Stephen KELLAM ◽  
Carol A. WRIGHT
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
High Performance ◽  
High Mobility ◽  
High Mobility Group ◽  
Transformed Cells ◽  
Hmg Proteins ◽  
Chromosomal Proteins

Separation of high-molecular mass RNAs by high-performance liquid chromatography on hydroxyapatite

1990 ◽  
Vol 515 ◽  
pp. 611-619 ◽  
Author(s):  
Shinichiro Hori ◽  
Sachiko Ohtani ◽  
Kenji Miyazaka ◽  
Toshihiro Ishikawa ◽  
Hitoshi Tanabe
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
High Performance ◽  
High Molecular Mass

scholarly journals Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence.

1991 ◽  
Vol 11 (1) ◽  
pp. 166-174 ◽  
Author(s):  
I G Schulman ◽  
T Wang ◽  
M Wu ◽  
J Bowen ◽  
R G Cook ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Tetrahymena Thermophila ◽  
High Mobility ◽  
Amino Acid Sequences ◽  
High Mobility Group ◽  
Binding Motif ◽  
Hmg Proteins ◽  
Chromosomal Proteins ◽  
Conserved Sequence

HMG (high-mobility-group protein) B and HMG C are abundant nonhistone chromosomal proteins isolated from Tetrahymena thermophila macronuclei with solubilities, molecular weights, and amino acid compositions like those of vertebrate HMG proteins. Genomic clones encoding each of these proteins have been sequenced. Both are single-copy genes that encode single polyadenylated messages whose amounts are 10 to 15 times greater in growing cells than in starved, nongrowing cells. The derived amino acid sequences of HMG B and HMG C contain a highly conserved sequence, the HMG 1 box, found in vertebrate HMGs 1 and 2, and we speculate that this sequence may represent a novel, previously unrecognized DNA-binding motif in this class of chromosomal proteins. Like HMGs 1 and 2, HMGs B and C contain a high percentage of aromatic amino acids. However, the Tetrahymena HMGs are small, are associated with nucleosome core particles, and can be specifically extracted from macronuclei by elutive intercalation, properties associated with vertebrate HMGs 14 and 17, not HMGs 1 and 2. Thus, it appears that these Tetrahymena proteins have features in common with both of the major subgroups of higher eucaryotic HMG proteins. Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box. This finding suggests that at least in T. thermophila, proteins with HMG-like properties are not restricted to regions of transcriptionally active chromatin.

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