Translational regulation of human methionine synthase by upstream open reading frames

Biochimica et Biophysica Acta - Gene Structure and Expression

Volumn 1769, Issue 9-10, 2007, Pages 532-540

  Col, Bekir ^a   Oltean, Sebastian ^a   Banerjee, Ruma ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Gene regulation; Methionine; Methionine synthase; Upstream open reading frame

Indexed keywords

ARGININE; METHIONINE SYNTHASE; POLYPEPTIDE; PROLINE; TIMONACIC ARGININE;

ANIMAL CELL; ARTICLE; CODON; CONTROLLED STUDY; DOWN REGULATION; GENE CONTROL; GENE MUTATION; HOUSEKEEPING GENE; HUMAN; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; RIBOSOME; RNA TRANSLATION; TRANSLATION REGULATION;

5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE S-METHYLTRANSFERASE; ANIMALS; CERCOPITHECUS AETHIOPS; CODON, INITIATOR; COS CELLS; DOWN-REGULATION; HUMANS; MUTATION; OPEN READING FRAMES; PROTEIN BIOSYNTHESIS;

EID: 34548659178     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2007.06.003     Document Type: Article

References (28)

1. Zou C.-G., and Banerjee R. Homocysteine and Redox Signaling. Antioxid. Redox Signal. 7 (2005) 547-559
2. Finkelstein J.D. Methionine metabolism in mammals. J. Nutr. Biochem. 1 (1990) 228-237
3. Swanson D.A., Liu M.L., Baker P.J., Garrett L., Stitzel M., Wu J., Harris M., Banerjee R., Shane B., and Brody L.C. Targeted disruption of the methionine synthase gene in mice. Mol. Cell. Biol. 21 (2001) 1058-1065
4. Boushey C.J., Beresford S.A., Omenn G.S., and Motulsky A.G. A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes. JAMA 274 (1995) 1049-1057
5. Mills J.L., McPartlin J.M., Kirke P.N., Lee Y.J., Conle M.R., and Weir D.G. Homocysteine metabolism in pregnancies complicated by neural tube defects. Lancet 345 (1995) 149-151
6. Clarke R., Smith A.D., Jobst K.A., Refsum H., Sutton L., and Ueland P.M. Folate, vitmain B12, and serum total homocysteine levels in confirmed Alzheimer's disease. Arch. Neruol. 55 (1998) 1449-1455
7. Hershey J.W.B., and Merrick W.C. The pathway and mechanism of initiation of protein synthesis. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). Translational Control of Gene Expression (2000), Cold Spring Harbor Laboratory Press, New York 33-88
8. Oltean S., and Banerjee R. Translational regulation of human methionine synthase by vitamin B12. J. Biol. Chem. 278 (2003) 20778-20784
9. Mangum J.H., and North J.A. Vitamin B12-dependent methionine biosynthesis in HEp-2 cells. Biochem. Biophys. Res. Commun. 32 (1968) 105-110
10. Mangum J.H., Murray B.K., and North J.A. Vitamin B12 dependent methionine biosynthesis in cultured mammalian cells. Biochemistry 8 (1969) 3496-3499
11. Gulati S., Brody L.C., and Banerjee R. Post transcriptional regulation of mammalian methionine synthase by B12. BBRC 259 (1999) 436-442
12. Oltean S., and Banerjee R. A B12-responsive IRES element in human methionine synthase. J. Biol. Chem. 280 (2005) 32662-32668
13. Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15 (1987) 8125-8148
14. Morris D.R., and Geballe A.P. Upstream open reading frames as regulators of mRNA translation. Mol. Cell. Biol. 20 (2000) 8635-8642
15. Morris D.R. Growth control of translation in mammalian cells. Prog. Nucleic Acid Res. Mol. Biol. 51 (1995) 339-363
16. Lavner Y., and Kotlar D. Codon bias as a factor in regulating expression via translation rate in the human genome. Gene 345 (2005) 127-138
17. Vilela C., Linz B., Rodrigues-Pousada C., and McCarthy J.E. The yeast transcription factor genes YAP1 and YAP2 are subject to differential control at the levels of both translation and mRNA stability. Nucleic Acids Res 26 (1998) 1150-1159
18. Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene 234 (1999) 187-208
19. Hinnesbusch A.G. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2. In: Hershey J.W.B., Mathews M.B., and Sonenberg N. (Eds). Tanslational Control (1996), Cold Spring Harbor Press, New York 199-244
20. Hill J.R., and Morris D.R. Cell-specific translation of S-adenosylmethionine decarboxylase mRNA. Regulation by the 5′ transcript leader. J. Biol. Chem. 267 (1992) 21886-21893
21. Ruan H., Hill J.R., Fatemie-Nainie S., and Morris D.R. Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Influence of the structure of the 5′ transcript leader on regulation by the upstream open reading frame. J. Biol. Chem. 269 (1994) 17905-17910
22. Geballe A.P., and Sachs M.S. Translational control by upstream open reading frames, in translational control of gene expression. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds) (2000), Cold Spring Harbor Press, Cold Spring Harbor, NY 595-614
23. Wang Z., and Sachs M.S. Ribosome stalling is responsible for arginine-specific translational attenuation in Neurospora crassa. Mol. Cell. Biol. 17 (1997) 4904-4913
24. Olivares-Trejo J.J., Bueno-Martinez J.G., Guarneros G., and Hernandez-Sanchez J. The pair of arginine codons AGA AGG close to the initiation codon of the lambda int gene inhibits cell growth and protein synthesis by accumulating peptidyl-tRNAArg4. Mol. Microbiol. 49 (2003) 1043-1049
25. Gaba A., Wang Z., Krishnamoorthy T., Hinnebusch A.G., and Sachs M.S. Physical evidence for distinct mechanisms of translational control by upstream open reading frames. EMBO J. 20 (2001) 6453-6463
26. Yaman I., Fernandez J., Liu H., Caprara M., Komar A.A., Koromilas A.E., Zhou L., Snider M.D., Scheuner D., Kaufman R.J., and Hatzoglou M. The zipper model of translational control: a small upstream ORF is the switch that controls structural remodeling of an mRNA leader. Cell 113 (2003) 519-531
27. Kent W.J., Sugnet C.W., Furey T.S., Roskin K.M., Pringle T.H., Zahler A.M., and Haussler D. The human genome browser at UCSC. Genome Res. 12 (2002) 996-1006
28. Kent W.J. BLAT-The BLAST-like alignment tool. Genome Res. 12 (2002) 656-664