Primary structure of non-histone protein HMG1 revealed by the nucleotide sequence

Tsuda, Kohichiroh; Kikuchi, Masahiro; Mori, Kazuyuki; Waga, Shiro; Yoshida, Michiteru

doi:10.1021/bi00416a050

Cited by 98 publications

(74 citation statements)

References 28 publications

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“…There is 80.4% homology between HMG1 (214 amino acid residues) and HMG2 (209 amino acid residues), which contain lysine-rich sequences in their HMG box domains A (positions and B (positions 94-162). 18,19) It seems, therefore, that GL has a high affinity with HMG1/2, as has been demonstrated for histones (H2A and H2B) 20) and lactoferrin, 12) which have arginine-and lysine-rich domains. These characteristics of gbPs containing arginine-and lysine-rich domains are correlated closely with the observations that (i) GL has a high affinity with DNA-binding proteins, including HMG1/2 (Fig.…”

Section: Discussionmentioning

confidence: 66%

Inhibitory Effect of Glycyrrhizin on the Phosphorylation and DNA-Binding Abilities of High Mobility Group Proteins 1 and 2 in Vitro.

Sakamoto

Okano

Takena

et al. 2001

Biological & Pharmaceutical Bulletin

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Recently, we reported that (i) casein kinase I (CK-I) specifically phosphorylates threonine residues on high mobility group protein 1 (HMG1) when incubated with cholesterol-3-sulfate (CH-3S); and (ii) CH-3S directly induces a drastic conformational change in HMG1.1) The latter finding provides a mechanism to explain how CH-3S alone can induce the phosphorylation of HMG1 by CK-I in vitro.HMG1 and HMG2 (HMG1/2) are abundant components of chromatin and a subfamily of the HMG proteins containing the HMG1 box domains is widely distributed in eukaryotic cells from yeast to human.2) It has been reported that (i) both HMG1/2 play important roles in the modulation of transcription, DNA integration and recombinations 2) ; (ii) cdc-2-kinase phosphorylates HMG1, and this phosphorylation reduces its DNA-binding affinity in vitro 3) ; (iii) Chironomus HMG1 4) and mouse testis-specific HMG1 5) are phosphorylated by protein kinase C (PKC) and appear to be required for the functioning of DNA-binding proteins, including topoisomerase I-dependent supercoiling activities 5) ; and (iv) HMG1 in Drosophila embryos and in the cultured cells of Chironomus is phosphorylated by CK-II at multiple serine residues located within the acidic tails, and this phosphorylation is important for the proper functioning and turnover rates of HMG1. 6) However, the physiological significance of the phosphorylation of HMG1/2 by these protein kinases (CK-I, CK-II and PKC) in the regulation of inflammatory mediators is not clear in present.Glycyrrhizin (GL) is present in large quantities in the roots and rhizomes of licorice, Glycyrrhiza glabra L., and is composed of a molecule of glycyrrhetinic acid (GA) and two molecules of glucuronic acid. We have been studying the physiological characteristics of the GL-binding proteins (gbPs) involved in inflammatory responses and the inhibitory effect of GL on gbP activities in vitro.7-12) Previously, we reported that (i) CK-II from mouse liver is selectively purified by GL-affinity column chromatography (HPLC) as a gbP 7) ; (ii) GL selectively inhibits the CK-II-mediated phosphorylation of cellular functional gbPs, such as glucocorticoid receptor, 7) lipoxygenase 3, 8) phospholipase A 2 (PLA 2 ) 9) and HIV-1 reverse transcriptase, 10,11) in vitro; and (iii) a GA derivative (oGA) is a potent inhibitor at one tenth the concentration of GL to inhibit the CK-II-mediated phosphorylation of these gbPs, 11) and also inhibiting the PKC-mediated phosphorylation of lactoferrin-binding proteins (angiogenin-1 and lactogenin-like protein) in vitro. 12)To investigate the physiological correlation between GL, HMG1/2 and three protein kinases (CK-I, CK-II and PKC) in vitro, we set out to (i) characterize HMG1/2 from a 0.35 M NaCl extract of calf thymus as gbPs with substrate activities for these protein kinases; (ii) characterize GL, GA and oGA as potent inhibitors of the phosphorylation of HMG1/2 by these protein kinases in vitro; and (iii) determine the inhibitory effect of GL on the DNA-binding ability of HMG1 in vitro. Enzymes ...

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Section: Discussionmentioning

confidence: 66%

Inhibitory Effect of Glycyrrhizin on the Phosphorylation and DNA-Binding Abilities of High Mobility Group Proteins 1 and 2 in Vitro.

Sakamoto

Okano

Takena

et al. 2001

Biological & Pharmaceutical Bulletin

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“…3). The homologous region in these cases matches the HMG box (Jantzen et al 1990;Kolodrubetz 1990), which corresponds to the conserved domains in nuclear high-mobility group protein HMG1 (Tsuda et al 1988;Wen et al 1989) and has been demonstrated to be a DNA-binding domain in some of the family members (Wright and Dixon 1988;Jantzen et al 1990). These suggest that Stell also could be a DNAbinding protein.…”

Section: Structure Of the Stel 1 Genementioning

confidence: 77%

“…Apparently, stel 1 regulates these genes positively. 91) is aligned with the following homologs: product of the S. pom be mating-type gene m atMc, amino acid residues 95-181 (Kelly et al 1988); putative human testis-determining factor (TDF), amino acid residues 71-158 ); porcine nuclear high-mobility group protein HMG1 (middle segment), amino acid residues 86-172 (Tsuda et al 1988); S. cerevisiae nonhistone chromosomal protein NHP6A, amino acid residues 12-92 (Kolodrubetz and Burgum 1990); human nucleolar transcription factor (hUBF)(upstream binding factor), amino acid residues 104-191 (Jantzen et al 1990}. Amino acids identical or conserved between Stel 1 and at least two of the homologs are shown in white against black, whereas those identical or conserved in three or more of the homologs but not in Stel 1 are shown in white against gray.…”

Section: Stel 1 Is Inducible By Nitrogen Starvation and Repressible Bmentioning

confidence: 99%

Schizosaccharomyces pombe ste11+ encodes a transcription factor with an HMG motif that is a critical regulator of sexual development.

et al. 1991

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Schizosaccharomyces pombe stell encodes a member of the family of HMG-box proteins. Its transcript is induced in response to nitrogen starvation and a concomitant decrease of the intracellular cAMP level. Expression of stell is essential for induction of sexual development, and its ectopic expression stimulates uncontrolled mating and sporulation. Stel 1 protein regulates positively transcription of the following genes required for sexual development: the mating type genes, matP and matM, and the mei2 gene, which is essential for commitment to meiosis. Stel 1 protein synthesized in vitro binds specifically to a DNA fragment carrying a 10-base motif TTCTTTGTTY that is an essential c/s-acting element for the induction of mei2 and is commonly seen in the upstream regions of the genes inducible by nitrogen starvation. These observations strongly suggest that Stel 1 serves as a key transcription factor for sexual development.

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“…Activators can also stimulate transcription indirectly by reversing the inhibitory effects of chromatin. Anionic regions rich in aspartic acid and glutamic acid residues are characteristic of many proteins that interact with chromatin, such as nucleoplasmin (8) and HMG1 (53). The acidic activator Gal4 can displace a nucleosome from the GAL1 promoter in vivo (2).…”

Section: Discussionmentioning

confidence: 99%

Involvement of Negative Cofactor NC2 in Active Repression by Zinc Finger-Homeodomain Transcription Factor AREB6

Ikeda

Halle

Stelzer

et al. 1998

Molecular and Cellular Biology

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The transcription factor AREB6 contains a homeodomain flanked by two clusters of Krüppel type C 2 H 2 zinc fingers. AREB6 binds to the E-box consensus sequence, CACCTGT, through either the N-or the C-terminal zinc finger cluster. To gain insights into the molecular mechanism by which AREB6 activates and represses gene expression, we analyzed the domain structure of AREB6 in the context of a heterologous DNA-binding domain by transient-transfection assays. The C-terminal region spanning amino acids 1011 to 1124 was identified as a conventional acidic activation domain. The region containing amino acids 754 to 901, which was identified as a repression domain, consists of 40% hydrophobic amino acids displaying no sequence similarities to other known repression domains. This region repressed transcription in vitro in a HeLa nuclear extract but not in reconstituted transcription systems consisting of transcription factor IID (TFIID), TFIIB, TFIIE, TFIIH/F, and RNA polymerase II. The addition of recombinant negative cofactor NC2 (NC2␣/DRAP1 and NC2␤/Dr1) to the reconstituted transcription system restored the activity of the AREB6 repression domain. We further demonstrated interactions between the AREB6 repression domain and NC2␣ in yeast two-hybrid assay. Our findings suggest a mechanism of transcriptional repression that is mediated by the general cofactor NC2.

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Primary structure of non-histone protein HMG1 revealed by the nucleotide sequence

Cited by 98 publications

References 28 publications

Inhibitory Effect of Glycyrrhizin on the Phosphorylation and DNA-Binding Abilities of High Mobility Group Proteins 1 and 2 in Vitro.

Inhibitory Effect of Glycyrrhizin on the Phosphorylation and DNA-Binding Abilities of High Mobility Group Proteins 1 and 2 in Vitro.

Schizosaccharomyces pombe ste11+ encodes a transcription factor with an HMG motif that is a critical regulator of sexual development.

Involvement of Negative Cofactor NC2 in Active Repression by Zinc Finger-Homeodomain Transcription Factor AREB6

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