Home LiteratureArticle Details
PMID: 7489724 Published · ppublish English Journal Article

Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2.

The EMBO journal ·Vol. 14 ·No. 21 ·1995-11-01 ·Pages 5350-7

Iwai K, Klausner RD, Rouault TA

Abstract

Iron regulatory proteins (IRPs) regulate the expression of genes involved in iron metabolism whose transcripts contain RNA stem-loop motifs known as iron-responsive elements (IREs). When iron concentrations are low, IRPs bind to IREs in the 5' untranslated region (UTR) of transcripts where they repress translation, or the 3' UTR of transcripts where they inhibit degradation. The RNA binding activities of the homologous proteins IRP1 and IRP2 are both regulated post-translationally. The binding activity of IRP2 is regulated by the degradation of the protein when cells are iron-replete. Here, we demonstrate that a 73 amino acid sequence that corresponds to a unique exon in IRP2 contains a sequence required for rapid degradation in iron-replete cells. The deletion of this sequence eliminates the rapid turnover of IRP2, whereas the transfer of this sequence to the corresponding position in the homologous protein IRP1 confers the capacity for iron-dependent degradation upon IRP1. Site-directed mutagenesis has demonstrated that specific cysteines within the IRP2 exon are required for iron-dependent degradation. The degradation of IRP2 appears to be mediated by the proteasome in iron-replete cells. When degradation is prevented, the RNA binding activity of IRP2 is not regulated by iron concentration. Thus, degradation is required for the regulation of the RNA binding activity of IRP2.

MeSH Terms
Amino Acid Sequence Cysteine/chemistry,metabolism Exons/genetics Gene Deletion Humans Iron/metabolism Iron Regulatory Protein 1 Iron Regulatory Protein 2 Iron-Regulatory Proteins Molecular Sequence Data Mutagenesis, Site-Directed Protein Processing, Post-Translational RNA-Binding Proteins/chemistry,genetics,metabolism Sequence Analysis Tumor Cells, Cultured
Chemicals
Iron-Regulatory Proteins RNA-Binding Proteins Iron Iron Regulatory Protein 1 Iron Regulatory Protein 2 Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Iwai K
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.
Klausner R D
Rouault T A
References (32)
32 references, click to expand
  1. Molecular regulation of iron proteins.
    Baillieres Clin Haematol. 1994 Dec;7(4):763-85 PMID: 7881153
  2. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.
    Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8797-801 PMID: 8090726
  3. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin.
    Science. 1995 May 5;268(5211):726-31 PMID: 7732382
  4. Expression of a constitutive mutant of iron regulatory protein 1 abolishes iron homeostasis in mammalian cells.
    J Biol Chem. 1995 Jun 30;270(26):15451-4 PMID: 7541043
  5. Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP) and IRPB.
    RNA. 1995 Apr;1(2):155-63 PMID: 7585245
  6. Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction.
    Science. 1989 Apr 21;244(4902):357-9 PMID: 2711187
  7. Non-redox roles for iron-sulfur clusters in enzymes.
    Biofactors. 1989 Dec;2(2):77-86 PMID: 2696478
  8. Cyclin is degraded by the ubiquitin pathway.
    Nature. 1991 Jan 10;349(6305):132-8 PMID: 1846030
  9. Metal-catalyzed oxidation of proteins. Physiological consequences.
    J Biol Chem. 1991 Feb 5;266(4):2005-8 PMID: 1989966
  10. A regulated RNA binding protein also possesses aconitase activity.
    Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10109-13 PMID: 1946430
  11. Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster.
    Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7536-40 PMID: 1502165
  12. Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III.
    Science. 1992 Oct 16;258(5081):434-40 PMID: 1411536
  13. An iron-sulfur cluster plays a novel regulatory role in the iron-responsive element binding protein.
    Biometals. 1992 Autumn;5(3):131-40 PMID: 1421965
  14. Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation.
    J Biol Chem. 1992 Dec 5;267(34):24466-70 PMID: 1447194
  15. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination.
    Nature. 1992 Dec 10;360(6404):597-9 PMID: 1334232
  16. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding.
    Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11735-9 PMID: 1281544
  17. Regulating the fate of mRNA: the control of cellular iron metabolism.
    Cell. 1993 Jan 15;72(1):19-28 PMID: 8380757
  18. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor.
    Cell. 1993 Jul 30;74(2):357-69 PMID: 8393731
  19. Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements.
    J Biol Chem. 1993 Dec 25;268(36):27327-34 PMID: 8262972
  20. Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase.
    EMBO J. 1994 Jan 15;13(2):453-61 PMID: 7508861
  21. Iron regulatory factor--the conductor of cellular iron regulation.
    Blood Rev. 1993 Dec;7(4):251-8 PMID: 8130687
  22. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity.
    J Biol Chem. 1994 Sep 30;269(39):24252-60 PMID: 7523370
  23. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation.
    J Biol Chem. 1994 Dec 9;269(49):30904-10 PMID: 7983023
  24. Regulated degradation of the transcription factor Gcn4.
    EMBO J. 1994 Dec 15;13(24):6021-30 PMID: 7813440
  25. Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome.
    J Biol Chem. 1995 Feb 3;270(5):2344-51 PMID: 7836468
  26. Structure of the allosteric regulatory enzyme of purine biosynthesis.
    Science. 1994 Jun 3;264(5164):1427-33 PMID: 8197456
  27. Split genes and RNA splicing.
    Cell. 1994 Jun 17;77(6):805-15 PMID: 7516265
  28. Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor.
    J Biol Chem. 1994 Jul 1;269(26):17481-9 PMID: 8021254
  29. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation.
    Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7321-5 PMID: 8041788
  30. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules.
    Cell. 1994 Sep 9;78(5):761-71 PMID: 8087844
  31. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B.
    Cell. 1994 Sep 9;78(5):773-85 PMID: 8087845
  32. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding.
    Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):2499-503 PMID: 7708673
Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1995-11-01
Pages
5350-7
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394644
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com