Characterization of cDNA sequences corresponding to three distinct HMG-1 mRNA species in line CHO Chinese hamster cells and cell cycle expression of the HMG-1 gene

Lee, Kam-Len Daniel; Pentecost, Brian T.; D'Anna, Joseph A.; Tobey, Robert A.; Gurley, L.R.; Dixon, Gordon H.

doi:10.1093/nar/15.13.5051

Cited by 47 publications

(20 citation statements)

References 31 publications

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“…Also included are different HMG boxes present in the same protein. Thus, the first group contains the following HMG boxes: pig (Sus scrofa) HMG1 (Tsuda et al 1988), pig HMG2 (Shirakawa et al 1990), bovine (Bos taurus) HMG1 (Kaplan and Duncan 1988), human (Homo sapiens) HMG1 (Wen et al 1989), hamster (Mesocricetus auratus) HMG1 (Lee et al 1987), rat (Rattus norvegicus) HMG1 (Paonessa et al 1987), trout (Salmo gairdneri) HMGT (Pentecost et al 205 1985), drosophila (Drosophila melanogaster) HMGD (Wagner et al 1992), maize (Zea mays) HMG (Grasser and Feix 1991), soybean (Glycine max) HMG (Laux and Goldberg 1991), Babesia bovis NHP1 (Dalrymple and Peters 1992), yeast (Saccharomyces cerevisiae) NHP6 (Kolodrubetz and Burgum 1990), and tetrahymena (Tetrahymena thermophila) HMGB (Schulman et al 1991). The HMG boxes aligned in the second group are taken from pig HMG1, pig HMG2, trout HMGT, maize HMG, soybean HMG, yeast NHP6, tetrahymena HMGB, human SSRP1 (Bruhn et al 1992), human T160 (Shirakata et al 1991), human TCF1 (van de Wetering et al 1991), human TCFlot (Waterman et al 1991), mouse (Mus musculus) LEF1 (Travis et al 1991), fission yeast (Schizosaccharomyces pombe) Mc (Kelly et al 1988), neurospora (Neurospora crassa) mat a (Staben and Yanofsky 1990), rat IRE-ABP (Nasrin et al 1991), human SRY ), mouse Tdy (Gubbay et al 1990), the three originally noted HMG boxes of human UBF (Jantzen et al 1990), yeast ABF2 (Diffley and Stillman 1991), and human mt TF1 (Parisi and Clayton 1991).…”

Section: Resultsmentioning

confidence: 99%

Phylogenetic relationships of HMG box DNA-binding domains

Griess¹,

Rensing²,

Grasser³

et al. 1993

J Mol Evol

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HMG boxes were initially identified as DNA-binding domains of the human RNA polymerase I (pol I) transcription factor hUBF and the animal high-mobility-group (HMG) protein family HMG1. Since then, numerous sequences of HMG-box-containing HMG proteins and other DNA-binding proteins from several species have become available. By sequence comparisons of a selected range of HMG boxes from these proteins and the construction of phylogenetic trees we show that the HMG box is highly conserved between DNA-binding proteins of organisms from all three eukaryotic kingdoms and that HMG boxes are linked by distinct evolutionary relationships. In addition, most HMG boxes display comparable hydropathy profiles and amino acid arrangements, which could serve as nuclear targeting sequences.

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Section: Resultsmentioning

confidence: 99%

Phylogenetic relationships of HMG box DNA-binding domains

Griess¹,

Rensing²,

Grasser³

et al. 1993

J Mol Evol

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“…Taken together, these results suggest that HMG1 may play a significant role in controlling general aspects of gene expression by modifying chromatin structure, and as such, can be viewed as a higher order regulatory factor. A number of cDNAs encoding HMG1 have been characterized from animals and insects [ 17,22,46,50,51], but only two plant cDNAs encoding HMG proteins have been characterized [ 11,21 ].…”

Section: Introductionmentioning

confidence: 99%

Abundance of an mRNA encoding a high mobility group DNA-binding protein is regulated by light and an endogenous rhythm

Zheng

Bui²,

O’Neill³

1993

Plant Mol Biol

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A cDNA clone encoding an HMG1 protein from Pharbitis nil was characterized with regard to its sequence, genomic organization and regulation in response to photoperiodic treatments that control floral induction. The HMG1 cDNA contains an open reading frame of 432 nucleotides encoding a 144 amino acid protein of approximately 16 kDa. The predicted polypeptide has the characteristic conserved motifs of the HMG1 and HMG2 class of proteins including an N-terminal basic region, one of two HMG-box domains, and a polyacidic carboxy terminus. Within the HMG-box region, Pharbitis HMG1 deduced amino acid sequence shares 47%, 67% and 69% identity with its animal, maize, and soybean counterparts, respectively. Southern blot hybridization analysis suggests that HMG1 is a member of a multigene family. Analysis of mRNA abundance indicates that the HMG1 gene is expressed to higher levels in dark-grown tissue, such as roots, and at lower levels in light-grown tissue, such as cotyledons and stems. Following the transition to darkness, the levels of HMG1 mRNA in cotyledons were initially stable, however, after a lag time of 8 h or more, HMG1 mRNA increased in abundance to a peak level at 20 h. A second peak in mRNA levels was observed about 24 h later, indicating that the expression of the HMG1 gene is regulated by an endogenous circadian rhythm. Abundance of the HMG1 mRNA during a dark period was dramatically affected by brief light exposure (night break), a treatment which inhibits floral induction. These data indicate that the expression of HMG1 is regulated by both an endogenous rhythm and the light/dark cycle and are consistent with a role for HMG1 in maintaining patterns of circadian-regulated gene expression activated upon the transition from light to darkness.

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“…The size of the sequenced HMG-T1 cDNA was in good agreement with the size of HMG-T1 mRNA obtained by Northern-blotting. It is relevant to note that in the human genome, two HMG-1 mRNA species (approximately 1.4 kb and approximately 2.4 kb; Wen et al, 1989;Stros and Dixon, 1993) and in Chinese hamster ovary (CHO) cells three HMG-1 mRNA species (1.05, 1.45 and 2.45 kb; Lee et al, 1987) have been detected by Northern-blotting. The different sizes of the CHO HMG-1 mRNAs are related to the presence of several putative polyadenylation sites in the 3' UTR of its sequence (Lee et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

“…The cDNA sequences for HMG-1 proteins are now known from a number of organisms such as bovine (Pentecost and Dixon, 1984;Kaplan and Duncan, 1988), Chinese hamster (Lee et al, 1987), rat (Paonessa et al, 1987), mouse (Yotov and St-Amaud, 1992), pig (Tsuda et al, 1988) and human (Wen et al, 1989). However, the only HMG-1 genomic sequpce so far described is a human HMG-1 retropseudogene (Stros and Dixon, 1993).…”

mentioning

confidence: 99%

cDNA sequence and structure of a gene encoding trout testis high‐mobility‐group‐1 protein

Štros

Nishikawa

Dixon

1994

European Journal of Biochemistry

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Perchloric acid extraction of trout testis nuclei revealed the presence of two large high-mobilitygroup (HMG) proteins, HMG-T1 and HMG-T2. The sequence of a complete cDNA (1407 bp) for trout testis HMG-1 protein (referred as to HMG-T1) has been determined. The deduced HMG-T1 protein contains 203 amino acids with more than 86% similarity to mammalian HMG-1 proteins. A single-sized mRNA for HMG-T1 has been detected by Northern-blot analysis consistent with the size derived from the HMG-T1 cDNA. Amplification of human and trout genomic DNAs by polymerase chain reaction using primers specific for trout and human HMG-1 cDNAs revealed that unlike the human genome, which contains predominantly intronless HMG-1 sequences, intronless HMG-T1 sequences were not found in the fish genome. Southern-blot analysis suggested that the trout testis HMG-1 gene is encoded by at least two sequences with high similarity.

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Characterization of cDNA sequences corresponding to three distinct HMG-1 mRNA species in line CHO Chinese hamster cells and cell cycle expression of the HMG-1 gene

Cited by 47 publications

References 31 publications

Phylogenetic relationships of HMG box DNA-binding domains

Phylogenetic relationships of HMG box DNA-binding domains

Abundance of an mRNA encoding a high mobility group DNA-binding protein is regulated by light and an endogenous rhythm

cDNA sequence and structure of a gene encoding trout testis high‐mobility‐group‐1 protein

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