Dinucleotide-binding site of bovine liver catalase mimics a catalase mRNA-binding protein domain

American Journal of Physiology - Lung Cellular and Molecular Physiology

Volumn 270, Issue 5 14-5, 1996, Pages

  Clerch, Linda Biadasz ^a   Wright, Angelique ^a   Massaro, Donald ^a  

^a GEORGETOWN UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Antioxidant enzyme; Reduced nicotinamide adenine dinucleotide phosphate

Indexed keywords

BINDING PROTEIN; CATALASE; DINUCLEOTIDE; MESSENGER RNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; LIVER; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN RNA BINDING;

ANIMALS; BASE SEQUENCE; BINDING SITES; CATALASE; CATTLE; DINUCLEOTIDE REPEATS; LIVER; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; NADP; NUCLEOCYTOPLASMIC TRANSPORT PROTEINS; NUCLEOTIDES; OLIGONUCLEOTIDE PROBES; RATS; RNA, MESSENGER; RNA-BINDING PROTEINS;

EID: 0029943702     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1996.270.5.l790     Document Type: Article

References (16)

1. Chu, E., D. M. Koeller, J. L. Casey, J. C. Drake, B. A. Chabner, P. C. Elwood, S. Zinn, and C. J. Allegra. Auto-regulation of human thymidylate synthase messenger RNA translation by thymidylate synthase. Proc. Natl. Acad. Sci. USA 88: 8977-8981, 1991.
2. Chu, E., C. H. Takimoto, D. Voeller, J. L. Grem, and C. J. Allegra. Specific binding of human dihydrofolate reductase protein to dihydrofolate reductase messenger RNA in vitro. Biochemistry 32: 4756-4760, 1993.
3. Clerch, L. B. A 3′ untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69 kDa redox-sensitive protein. Arch. Biochem. Biophys. 317: 267-274, 1995.
4. Clerch, L. B., J. Iqbal, and D. Massaro. Perinatal rat lung catalase gene expression: influence of corticosteroid and hyperoxia. Am. J. Physiol. 260 (Lung Cell. Mol. Physiol. 4): L428-L433, 1991.
5. Clerch, L. B., and D. Massaro. Tolerance of rats to hyperoxia-lung antioxidant gene expression. J. Clin. Invest 91: 499-508, 1993.
6. Clerch, L. B., and D. Massaro. Oxidation-reduction sensitive binding of lung protein to rat catalase mRNA. J. Biol. Chem. 267: 2853-2855, 1992.
7. Fita, I., and M. G. Rossmann. The NADPH binding site on beef liver catalase. Proc. Natl. Acad. Sci. USA 82: 1604-1608, 1985.
8. Furuta, S., H. Hayashi, M. Huikata, S. Miyazawa, T. Osumi, and T. Hashimoto. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc. Natl. Acad. Sci. USA 83: 313-317, 1986.
9. Hentze, M. W. Enzymes as RNA-binding proteins: a role for (di)nucleotide-binding domains? Trends Biol. Sci. 19: 101-103, 1994.
10. Jouve, H. M., J. Pelmont, and J. Gaillard. Interaction between pyridine adenine dinucleotides and bovine liver catalase: a chromatographic and spectral study. Arch. Biochem Biophys. 248: 71-79, 1986.
11. Kirkman, H. N., and G. F. Gaetani. Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci. USA 81: 4343-4347, 1984.
12. Kirkman, H. N., S. Galiano, and G. F. Gaetani. The function of catalase-bound NADPH. J. Biol. Chem. 262: 660-666, 1987.
13. Klausner, R. D., T. A. Rouault, and J. B. Harford. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72: 19-28, 1993.
14. Mashino, T., and I. Fridovich. NADPH mediates the inactivation of bovine liver catalase by monochloroamine. Arch. Biochem. Biophys. 265: 279-285, 1988.
15. Yen, T. J., P. S. Machlin, and D. W. Cleveland. Autoregulated instability of beta-tubulin mRNAs by recognition of the nascent amino terminus of beta-tubulin. Nature Lond. 334: 580-585, 1988.
16. Zuker, M. On finding all suboptimal foldings of an RNA molecule. Science Wash. DC 244: 48-52, 1989.