Fine structure and evolution of the rat serum albumin gene.

Sargent, Thomas D.; Jagodzinski, Linda L.; Yang, Mian; Bonner, Jr W D

doi:10.1128/mcb.1.10.871

Cited by 112 publications

(55 citation statements)

References 19 publications

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“…Like the HNF1 site, the NF-Y region contributed little direct promoter stimulation. This is particularly clear The mouse albumin promoter sequences from rat (66), mouse (28), human (67), and cow (68) are aligned along with the synthetic promoter Alb123. Bases that are perfectly conserved among all species are shaded.…”

Section: Resultsmentioning

confidence: 99%

Distant Enhancers Stimulate the Albumin Promoter through Complex Proximal Binding Sites

Vorachek

Steppan

Lima

et al. 2000

Journal of Biological Chemistry

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The albumin-␣-fetoprotein locus epitomizes the main features of transcriptional regulation of fetal and adult hepatocyte-specific genes: developmentally regulated promoters and strong distant enhancers. Full enhancer activity required only a proximal albumin-promoter region containing the TATA box, hepatic nuclear factor 1 (HNF1), and nuclear factor Y (NF-Y) sites. Deletion of the HNF1 site abrogated enhancer and promoter activity, whereas methylation of the site reduced all activity by about 3-fold. Deletion of the NF-Y site attenuated activity by about half, but much of the activity could be replaced by juxtaposition of an upstream region (designated distal element IV). Gel shift and competition analysis demonstrated that binding of architectural factors overlapped NF-Y binding. Moreover, a mutation that eliminated NF-Y binding but only minimally perturbed the surrounding region did not affect enhancer function. In plasmids with a second promoter, the enhancers simultaneously stimulated both albumin and ␣-fetoprotein promoters with minimal competition, but surprisingly some mutations in the albumin promoter attenuated expression from both promoters, whereas another uncoupled their expression. With single promoters, the function of the proximal promoter region was controlled by three parameters in the following hierarchy: HNF1 binding > local architecture > NF-Y binding, but integrated two-promoter function had a much greater dependence on NF-Y.

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Section: Resultsmentioning

confidence: 99%

Distant Enhancers Stimulate the Albumin Promoter through Complex Proximal Binding Sites

Vorachek

Steppan

Lima

et al. 2000

Journal of Biological Chemistry

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“…All the protein sequence and gene structure (human, mouse, and rat albumin: Minghetti et al, 1986;Sargent et al, 1981a;mouse alpha-fetoprotein: Gorin & Tilghman, 1980;Eiferman et al, 1981) data collected for the three members of this multigene family support the view that plasma albumin was at one time a single domain of about 190 amino acids. Through quantitative amino acid sequence comparisons, it is apparent that albumins and alpha-fetoproteins are more similar to each other than either is to the vitamin D-binding proteins.…”

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confidence: 84%

Characterization, primary structure, and evolution of lamprey plasma albumin

Gray

Doolittle

1992

Protein Science

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The most abundant protein found in blood plasma from the sea lamprey (Petromyzon marinus) has the hallmarks of a plasma albumin: namely, high abundance, solubility in distilled water, a small number of tryptophans, and a high content of cysteines and charged residues. As in other vertebrate albumins, not all the cysteines are disulfide bonded. An unusual feature of this protein is its molecular weight of 175,000, roughly 2.5 times the size of other vertebrate albumins. Its amino acid sequence, deduced from a series of overlapping cDNA clones, can be aligned with other members of the gene family including plasma albumin, alpha-fetoprotein, and vitamin-D binding protein, confirming that it is indeed an oversized albumin. An unusual feature of the sequence is a 28-amino acid stretch consisting of a serine-threonine repeat with the general motif (STTT). Lamprey albumin contains a 23-amino acid putative signal peptide and a 6-residue putative propeptide, which, when cleaved, yield a mature protein of 1,394 amino acids with a calculated molecular weight of 157,000. The sequence also includes nine potential N-linked glycosylation sites (Asn-X-Ser/Thr), consistent with observation that lamprey albumin is a glycoprotein. If all the potential glycosylation sites were occupied by clusters of 2,000 molecular weight each, the total molecular weight would be 175,000. Like other members of the gene family, lamprey albumin is composed of a series of 190-amino acid repeats, there being seven such domains all together. Quantitative amino acid sequence comparisons of lamprey albumin with the other members of the gene family indicate that it diverged from an ancestral albumin prior to the gene duplications leading to this diverse group. This notion is confirmed by the pattern of amino acid insertions and deletions observed in a consideration of all domains that compose this family. Furthermore, it suggests that the invention of albumin antedates the vertebrate radiation.Keywords: plasma albumin; protein evolution; sea lamprey Plasma albumin is the most abundant protein in vertebrate blood plasma and also among the most readily purified. The ability to secure relatively pure albumin in large quantities has led to it becoming one of the most familiar and extensively studied of all proteins. Its principal role is thought to be that of a transport protein, reversibly binding fatty acids, bilirubin, and a myriad of other molecules, as well as its being a major contributor to the effective osmotic pressure of the plasma. As a result of its ligand-binding properties and high concentration, albumin provides a stabilizing effect on plasma solute levels, buffering the concentration of metabolites. Paradoxically, humans and some other animals appear to be quite capable of surviving with levels of albumin in

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“…Transcripts derived from repetitive and single-copy sequences have been described in many systems. The silk fibroin (16), dihydrofolate reductase (6), vitellogenin (23), albumin (18), CAD (15), and cortico-p-lipoprotein (22) genes contain repetitive elements within intervening sequences, whereas their mature mRNAs are essentially single copy. In sea urchins, the maternal RNA population is composed largely of compound transcripts, although many of these maternal transcripts appear to be unprocessed pre-mRNAs (17).…”

Section: Discussionmentioning

confidence: 99%