scholarly journals Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein.

1991 ◽  
Vol 266 (30) ◽  
pp. 19945-19952 ◽  
Author(s):  
M.S. Nissen ◽  
T.A. Langan ◽  
R. Reeves
Keyword(s):  
Dna Binding ◽  
High Mobility ◽  
Binding Activity ◽  
High Mobility Group ◽  
Chromatin Protein ◽  
Cdc2 Kinase ◽  
Dna Binding Activity ◽  
Group I

scholarly journals Glutamine attenuates acute lung injury by inhibition of high mobility group box protein-1 expression during sepsis

2009 ◽  
Vol 103 (6) ◽  
pp. 890-898 ◽  
Author(s):  
Woon Yong Kwon ◽  
Gil Joon Suh ◽  
Kyung Su Kim ◽  
You Hwan Jo ◽  
Jae Hyuk Lee ◽  
...  
Keyword(s):  
Acute Lung Injury ◽  
Heat Shock ◽  
Dna Binding ◽  
Lung Injury ◽  
High Mobility ◽  
Binding Activity ◽  
Negative Regulator ◽  
High Mobility Group ◽  
Hsp70 Expression ◽  
Dna Binding Activity

Heat shock protein 70 (HSP70) is reported as the main factor responsible for the beneficial effects of glutamine (GLN) and as a negative regulator of high mobility group box protein-1 (HMGB-1) expression. Our aim was to determine whether GLN attenuates acute lung injury (ALI) by the inhibition of HMGB-1 expression during sepsis. Male Sprague–Dawley rats were subjected to caecal ligation and puncture (CLP) to induce sepsis. GLN or saline was administered through tail vein 1 h after CLP. Then, quercetin (Q), an inhibitor of HSP70, was utilised to assess the role of the enhanced HSP70. We observed the survival of the subjects. At 24 h post-CLP, we measured lung HSP70, phosphorylated heat shock factor-1 (HSF-1-p) and HMGB-1 expressions, NF-κB DNA-binding activity and ALI occurrence. We also measured serum HSP70, IL-6 and HMGB-1 concentrations. GLN improved survival during sepsis. In GLN-treated rats, lung HSP70 and HSF-1-p expressions were enhanced, lung HMGB-1 expression and NF-κB DNA-binding activity were suppressed, and ALI was attenuated. Furthermore, in GLN-administered rats, serum HSP70 concentration was higher, and serum IL-6 and HMGB-1 concentrations were lower than those in non-treated rats. Q inhibited the enhancement of HSP70 and HSF-1-p expressions and abrogated the GLN-mediated benefits. In conclusion, GLN attenuated ALI and improved survival by the inhibition of HMGB-1 expression during sepsis in rats. These benefits were associated with the enhancement of HSP70 expression by GLN.

scholarly journals Inherited Human XY Sex Reversal and Gonadal Neoplasia Due to Enhanced Formation of Non-Specific Enhanceosomes by an Architectural Transcription Factor

2021 ◽  
Vol 5 (Supplement_1) ◽  
pp. A506-A506
Author(s):  
Yen-Shan Chen ◽  
Joseph D Racca ◽  
Alicia Belgorosky ◽  
Michael Aaron Weiss
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
High Mobility ◽  
Binding Activity ◽  
Wild Type ◽  
Cell Fates ◽  
Developmental Defects ◽  
Hmg Box ◽  
Dna Binding Activity ◽  
Gene Regulatory

Abstract The development of organisms is regulated by a fine-tuned gene-regulatory network, which is driven by transcription factors (TFs). In the embryogenesis, these TFs control diverse cell fates and final body plan. This is precisely regulated by a specific DNA-binding process and enhanceosome formation. A model is provided by testis determination in mammals, which is initiated by a Y-encoded architectural transcription factor, SRY. Mutations in SRY cause gonadal dysgenesis leading to various developmental defects. Such mutations cluster in SRY’s high mobility group (HMG) box, a sequence-specific DNA-binding domain shared by a conserved family of TFs. Here, we have characterized several mutations at the same position in HMG box, which are compatible with either male or female phenotypes as observed in an XY father and XY daughter, respectively. These mutations, at a function-unknown motif in the SRY HMG box, markedly disturb the specific DNA affinity. On transient transfection of human and rodent cell lines, the SRY variants exhibit decreased specific DNA-binding activity (relative to wild type) are associated with mis-formed enhanceosomes. The variants’ gene regulatory activities were reduced by 2-fold relative to wild-type SRY at similar levels of mRNA expression. When engineered mutations that functions to increase the DNA-binding specificity were deployed to SRY variants, the transcriptional activity was in association with restored occupancy of sex-specific enhancer elements in principal downstream gene Sox9. Our findings define a novel mechanism of impaired organogenesis, disturbed specific DNA-binding activity of a master transcription factor, leading to a developmental decision poised at the edge of ambiguity.

scholarly journals A testis-specific gene encoding a nuclear high-mobility-group box protein located in elongating spermatids.

1993 ◽  
Vol 13 (7) ◽  
pp. 4323-4330 ◽  
Author(s):  
G Boissonneault ◽  
Y F Lau
Keyword(s):  
Dna Binding ◽  
Regulation Of Gene Expression ◽  
High Mobility ◽  
Binding Activity ◽  
High Mobility Group ◽  
Immunocytochemical Staining ◽  
Specific Gene ◽  
Sequence Specificity ◽  
Mobility Shift ◽  
Hmg Protein

A cDNA encoding a DNA-binding protein has been isolated by screening a mouse testicular expression cDNA library with a concatemer of a 12-bp putative protein-binding element present in the promoter of the testis-specific gene PGK-2. Sequence analysis of the isolated cDNA indicated the presence of an open reading frame that encodes a protein with two conserved DNA-binding motifs known as the high-mobility-group (HMG) boxes. Northern (RNA) blot analysis demonstrated that expression of the gene is restricted to the postpuberal testis. The DNA-binding activity and sequence specificity of the recombinant HMG protein were confirmed by DNA mobility shift assay using the initial concatemer of the PGK-2 promoter element as a probe as well as the wild-type or mutated versions of the 12-bp element within its natural sequence context. Immunocytochemical staining of adult testis sections with polyclonal antisera recognizing this recombinant HMG protein demonstrated that it is located predominantly in the nuclei of elongated spermatids at steps 9 and 10. These results suggest that this novel HMG box protein gene may be involved in the regulation of gene expression of the haploid male genome. The gene from which the cDNA was derived has been termed testis-specific HMG (tsHMG).

A testis-specific gene encoding a nuclear high-mobility-group box protein located in elongating spermatids

1993 ◽  
Vol 13 (7) ◽  
pp. 4323-4330
Author(s):  
G Boissonneault ◽  
Y F Lau
Keyword(s):  
Dna Binding ◽  
Regulation Of Gene Expression ◽  
High Mobility ◽  
Binding Activity ◽  
High Mobility Group ◽  
Immunocytochemical Staining ◽  
Specific Gene ◽  
Sequence Specificity ◽  
Mobility Shift ◽  
Hmg Protein

A cDNA encoding a DNA-binding protein has been isolated by screening a mouse testicular expression cDNA library with a concatemer of a 12-bp putative protein-binding element present in the promoter of the testis-specific gene PGK-2. Sequence analysis of the isolated cDNA indicated the presence of an open reading frame that encodes a protein with two conserved DNA-binding motifs known as the high-mobility-group (HMG) boxes. Northern (RNA) blot analysis demonstrated that expression of the gene is restricted to the postpuberal testis. The DNA-binding activity and sequence specificity of the recombinant HMG protein were confirmed by DNA mobility shift assay using the initial concatemer of the PGK-2 promoter element as a probe as well as the wild-type or mutated versions of the 12-bp element within its natural sequence context. Immunocytochemical staining of adult testis sections with polyclonal antisera recognizing this recombinant HMG protein demonstrated that it is located predominantly in the nuclei of elongated spermatids at steps 9 and 10. These results suggest that this novel HMG box protein gene may be involved in the regulation of gene expression of the haploid male genome. The gene from which the cDNA was derived has been termed testis-specific HMG (tsHMG).

scholarly journals Physical interaction of tumour suppressor p53/p73 with CCAAT-binding transcription factor 2 (CTF2) and differential regulation of human high-mobility group 1 (HMG1) gene expression

2003 ◽  
Vol 371 (2) ◽  
pp. 301-310 ◽  
Author(s):  
Hidetaka URAMOTO ◽  
Hiroto IZUMI ◽  
Gunji NAGATANI ◽  
Haruki OHMORI ◽  
Naofumi NAGASUE ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Replication ◽  
Dna Binding ◽  
Promoter Activity ◽  
High Mobility ◽  
Binding Activity ◽  
Physical Interaction ◽  
Dna Binding Activity ◽  
P21 Promoter ◽  
Group 1

The CCAAT-binding transcription factor (CTF)/nuclear factor I (NF-I) group of cellular DNA-binding proteins recognizes the sequence GCCAAT and is implicated in eukaryotic transcription, as well as DNA replication. Molecular analysis of human CTF/NF-I cDNA clones revealed multiple mRNA species that contain alternative coding regions, apparently as a result of differential splicing. Expression and functional analysis established that individual gene products can bind to GCCAAT recognition sites and serve as both promoter-selective transcriptional activators and initiation factors for DNA replication. The interaction between CTF2 and p53/p73 was shown to modulate their ability to regulate transcription of their respective target genes. In the present paper, we report that p53 down-regulates the activity of the high mobility group 1 (HMG1) gene promoter, whereas p73α up-regulates the activity of this promoter. Furthermore, CTF2 transactivates p53-induced p21 promoter activity, but inhibits p73α-induced p21 promoter activity. Using deletion mutants, we found that the DNA-binding domains of both p53 and p73α are required for physical interaction with CTF2 via the regions between amino acid residues 161 and 223, and 228 and 312 respectively. CTF2 enhances the DNA-binding activity of p53 and inhibits the DNA-binding activity of p73α. These results provide novel information on the functional interplay between CTF2 and p53/p73 as important determinants of their function in cell proliferation, apoptosis, DNA repair and cisplatin resistance.

scholarly journals High mobility group I(Y)-like DNA-binding domains on a bacterial transcription factor.

1996 ◽  
Vol 93 (14) ◽  
pp. 6881-6885 ◽  
Author(s):  
F. J. Nicolas ◽  
M. L. Cayuela ◽  
I. M. Martinez-Argudo ◽  
R. M. Ruiz-Vazquez ◽  
F. J. Murillo
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
High Mobility ◽  
High Mobility Group ◽  
Dna Binding Domains ◽  
Bacterial Transcription ◽  
Binding Domains ◽  
Group I

scholarly journals The first high-mobility-group box of upstream binding factor assembles across-over DNA junction by basic residues

1998 ◽  
Vol 333 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Chin-Hwa HU ◽  
Ju-Ming WANG ◽  
Hua-Bin TSENG
Keyword(s):  
Dna Binding ◽  
High Mobility ◽  
Dna Interaction ◽  
Binding Activity ◽  
High Mobility Group ◽  
Binding Motif ◽  
Dimerization Domain ◽  
Mobility Shift ◽  
Binding Factor ◽  
Upstream Binding Factor

Upstream binding factor (UBF) is a eukaryotic RNA polymerase I-specific transcription factor. Its predominant DNA-binding motif, ubfHMG box 1, preserves DNA assembling activity that can bind two or more DNA duplexes simultaneously to form a crossover DNA junction. Here we investigate the basis of crossover DNA-assembling activity of ubfHMG box 1 by extensive mutagenesis analyses and mobility shift assay. Although the ubfHMG box 1 preserves a high mobility group (HMG) core structure, changing a number of the consensus hydrophobic and aromatic residues to alanine did not inhibit its crossover-assembling activity. This indicates that these residues do not directly participate in protein–DNA interaction. However, altering a series of basic residues in the helices 1 and 2 regions or the N-terminal extended strand of the ubfHMG box 1 motif had severe effects on DNA-assembling activity; however, certain non-specific DNA binding activity still remained. This suggests that the ubfHMG box 1 motif might extensively contact the backbone of a crossover junction through its multiple basic residues. Mutating a hydrophobic residue in the terminal dimerization domain inhibited the association of truncated Xenopus UBF, but had little effect on its crossover-assembling activity. This indicates that the UBF–crossover DNA complex is not established by the association of individual DNA-bound peptides.

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