scholarly journals Canonical HMG Protein

2020 ◽  
Author(s):  
Keyword(s):  
Hmg Protein

scholarly journals Identification of genes encoding zinc finger proteins, non-histone chromosomal HMG protein homologue, and a putative GTP phosphohydrolase in the genome of Chilo iridescent virus

1994 ◽  
Vol 22 (2) ◽  
pp. 158-166 ◽  
Author(s):  
Paul Schnitzler ◽  
Michael Hug ◽  
Michaela Handermann ◽  
Waltraud Janssen ◽  
Eugene V. Koonin ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Chilo Iridescent Virus ◽  
Iridescent Virus ◽  
Genes Encoding ◽  
Hmg Protein

scholarly journals The Yeast HMG Protein HMO1 Alters Nucleosome Structure

2014 ◽  
Vol 106 (2) ◽  
pp. 74a-75a
Author(s):  
Micah J. McCauley ◽  
Ran Huo ◽  
Nicole Becker ◽  
Molly Nelson Holt ◽  
Uma Muthurajan ◽  
...  
Keyword(s):  
Nucleosome Structure ◽  
Hmg Protein

scholarly journals Specialization of the chromatin remodeler RSC to mobilize partially-unwrapped nucleosomes

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Alisha Schlichter ◽  
Margaret M Kasten ◽  
Timothy J Parnell ◽  
Bradley R Cairns
Keyword(s):  
Ribosomal Protein ◽  
Chromatin Remodeling ◽  
Dna Sequences ◽  
Dna Binding Proteins ◽  
Ribosomal Protein Genes ◽  
Expression Of Genes ◽  
Chromatin Remodeling Complexes ◽  
Hmg Protein ◽  
Better Than

SWI/SNF-family chromatin remodeling complexes, such as S. cerevisiae RSC, slide and eject nucleosomes to regulate transcription. Within nucleosomes, stiff DNA sequences confer spontaneous partial unwrapping, prompting whether and how SWI/SNF-family remodelers are specialized to remodel partially-unwrapped nucleosomes. RSC1 and RSC2 are orthologs of mammalian PBRM1 (polybromo) which define two separate RSC sub-complexes. Remarkably, in vitro the Rsc1-containing complex remodels partially-unwrapped nucleosomes much better than does the Rsc2-containing complex. Moreover, a rsc1Δ mutation, but not rsc2Δ, is lethal with histone mutations that confer partial unwrapping. Rsc1/2 isoforms both cooperate with the DNA-binding proteins Rsc3/30 and the HMG protein, Hmo1, to remodel partially-unwrapped nucleosomes, but show differential reliance on these factors. Notably, genetic impairment of these factors strongly reduces the expression of genes with wide nucleosome-deficient regions (e.g., ribosomal protein genes), known to harbor partially-unwrapped nucleosomes. Taken together, Rsc1/2 isoforms are specialized through composition and interactions to manage and remodel partially-unwrapped nucleosomes.

scholarly journals A high-mobility-group protein and its cDNAs from Drosophila melanogaster.

1992 ◽  
Vol 12 (5) ◽  
pp. 1915-1923 ◽  
Author(s):  
C R Wagner ◽  
K Hamana ◽  
S C Elgin
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosome 2 ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
Hmg Protein

We have identified, purified, and characterized a high-mobility-group (HMG) protein and its cDNAs from Drosophila melanogaster. This protein, HMG D, shares most of the characteristics of vertebrate HMG proteins; it is extractable from nuclei with 0.35 M NaCl, is soluble in 5% perchloric acid, is relatively small (molecular weight of 12,000), has both a high basic (24%) and high acidic (24%) amino acid content, and is a DNA-binding protein. HMG D exhibits characteristics of both the vertebrate HMG 1 and 2 class and the HMG 14 and 17 class of proteins. Its amino acid sequence is similar (36% amino acid identity) to that of HMG1, while its size and selective extraction with ethidium bromide are similar to properties of the HMG 14 and 17 class of proteins. HMG D is encoded by a single-copy gene that maps to 57F8-11 on the right arm of chromosome 2. Two transcripts are observed during embryogenesis; the protein is relatively stable throughout development. By the biochemical criteria of size, solubility, and amino acid content, HMG D appears to be the major HMG protein of D. melanogaster.

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