Literature DB >> 3584116

Characterization and evolution of the expressed rat ferritin light subunit gene and its pseudogene family. Conservation of sequences within noncoding regions of ferritin genes.

E A Leibold, H N Munro.   

Abstract

The iron storage protein ferritin consists of two types of subunits of different molecular weight, heavy (H) and light (L). The rat genome contains approximately 20 copies of the ferritin L-subunit gene, of which we have sequenced seven. One is an expressed ferritin gene containing three introns located between the alpha-helical domains of the L-subunit protein. The remaining six have the characteristics of processed pseudogenes. Sequence divergence suggest that these pseudogenes arose approximately 3-12 X 10(6) years ago, well within the 30 X 10(6) years of divergence of rat and mouse. By using intron probes derived from the expressed ferritin L-gene, a homologous second copy has been identified in some Fischer rats. Comparison of the 5'-untranslated region of the rat L-gene with the published sequences of this region of the human L (Santoro, C., Marone, M., Ferrone, M., Costanzo, F., Colombo, M., Minganti, C., Cortese, R., and Silengo, L. (1986) Nucleic Acids Res. 14, 2863-2876) and H (Costanzo, F., Colombo, M., Staempfli, S., Santoro, C., Marone, M., Frank, R., Delius, H., and Cortese, R. (1986) Nucleic Acids Res. 14, 721-735) genes and of a bullfrog cDNA (Didsbury, J. R., Theil, E. C., Kaufman, R. E., and Dickey, L. F. (1986) J. Biol. Chem. 261, 949-955) show a strongly conserved 28-base pair sequence, suggesting a translational regulatory function. The 5' flanking region of the rat L-gene contains sequences homologous to those in the flanking areas of the human L- and H-genes. The implications of these conserved sequences for control of ferritin expression are discussed.

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Year:  1987        PMID: 3584116

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  25 in total

1.  A second ferritin L subunit is encoded by an intronless gene in the mouse.

Authors:  F Renaudie; A K Yachou; B Grandchamp; R Jones; C Beaumont
Journal:  Mamm Genome       Date:  1992       Impact factor: 2.957

2.  An 'equalized cDNA library' by the reassociation of short double-stranded cDNAs.

Authors:  M S Ko
Journal:  Nucleic Acids Res       Date:  1990-10-11       Impact factor: 16.971

3.  From cis-regulatory elements to complex RNPs and back.

Authors:  Fátima Gebauer; Thomas Preiss; Matthias W Hentze
Journal:  Cold Spring Harb Perspect Biol       Date:  2012-07-01       Impact factor: 10.005

4.  Position is the critical determinant for function of iron-responsive elements as translational regulators.

Authors:  B Goossen; M W Hentze
Journal:  Mol Cell Biol       Date:  1992-05       Impact factor: 4.272

Review 5.  Molecular control of vertebrate iron homeostasis by iron regulatory proteins.

Authors:  Michelle L Wallander; Elizabeth A Leibold; Richard S Eisenstein
Journal:  Biochim Biophys Acta       Date:  2006-05-17

6.  The location of exon boundaries in the multimeric iron-storage protein ferritin.

Authors:  P M Harrison; G C Ford; J M Smith; J L White
Journal:  Biol Met       Date:  1991

Review 7.  Mammalian iron metabolism and its control by iron regulatory proteins.

Authors:  Cole P Anderson; Macy Shen; Richard S Eisenstein; Elizabeth A Leibold
Journal:  Biochim Biophys Acta       Date:  2012-05-17

8.  Genetic mapping of the mouse ferritin light chain gene and 11 pseudogenes on 11 mouse chromosomes.

Authors:  J D Filie; C E Buckler; C A Kozak
Journal:  Mamm Genome       Date:  1998-02       Impact factor: 2.957

9.  Perspectives on the ARE as it turns 25 years old.

Authors:  Daniel Beisang; Paul R Bohjanen
Journal:  Wiley Interdiscip Rev RNA       Date:  2012-06-25       Impact factor: 9.957

10.  Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis.

Authors:  Z Kikinis; R S Eisenstein; A J Bettany; H N Munro
Journal:  Nucleic Acids Res       Date:  1995-10-25       Impact factor: 16.971

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