Availability of a second upstream AUG can completely overcome inhibition of protein synthesis initiation engendered by mRNA secondary structure encompassing the start codon

Gene

Volumn 196, Issue 1-2, 1997, Pages 231-237

  Satchidanandam, Vijaya ^a   Shivashankar, Yuvarani ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Flaviviral protease; Northern analysis; Protein hyperexpression; Translation block

Indexed keywords

RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION; JAPANESE ENCEPHALITIS VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN RNA BINDING; PROTEIN SYNTHESIS INHIBITION; RNA STRUCTURE; RNA TRANSLATION; START CODON; VIRUS GENE;

AMINO ACID SEQUENCE; BASE SEQUENCE; CODON, INITIATOR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PROTEIN BIOSYNTHESIS; RECOMBINANT PROTEINS; RNA HELICASES; RNA, MESSENGER; SERINE ENDOPEPTIDASES; TRANSCRIPTION, GENETIC; VIRAL NONSTRUCTURAL PROTEINS;

ESCHERICHIA COLI; JAPANESE ENCEPHALITIS VIRUS;

EID: 0030769734     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00232-1     Document Type: Article

References (29)

1. Adhin, M.R., van Duin, J., 1990. Scanning model for translational reinitiation in eubacteria. J. Mol. Biol. 213, 811-818.
2. Bazan, J.F., Fletterick, R.J., 1989. Detection of a trypsin like serine protease domain in flaviviruses and pestiviruses. Virology 171, 637-639.
3. Chambers, T.J., Hahn, C.S., Galler, R., Rice, C.M., 1990. Flavivirus genome organization, expression and replication. Annu. Rev. Microbiol. 44, 649-688.
4. Chambers, T.J., Weir, R.C., Grakoui, A., McCourt, D.W., Bazan, J.F., Fletterick, R.J., Rice, C.M., 1990. Evidence that the N-terminal domain of the nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site specific cleavages in the viral polyprotein. Proc. Natl. Acad. Sci. USA. 87, 8898-8902.
5. Chambers, T.J., Grakoui, A., Rice, C.M., 1991. Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites. J. Virol. 65, 6042-6050.
6. Falgout, B., Pethel, M., Zhang, Y.M., Lai, C.J., 1991. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J. Virol. 65, 2467-2475.
7. Gold, L., 1988. Post transcriptional regulatory mechanisms in Escherichia coli. Annu. Rev. Biochem. 57, 199-233.
8. Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., 1989. N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res. 17, 4713-4729.
9. Hall, M.N., Gabay, J., Debarbouille, M., Schwartz, M., 1982. A role for mRNA secondary structure in the control of translation initiation. Nature (London) 295, 616-618.
10. Knight, J.A., Hardy, L.W., Rennel, D., Herrick, D., Poteete, A., 1987. Mutations in an upstream regulatory sequence that increase expression of the bacteriophage T4 lysozyme gene. J. Bacteriol. 169, 4630-4636.
11. Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
12. Lathrop, B.K., Burack, W.R., Biltonen, R.L., Rule, G.S., 1992. Expression of a group II phosholipase A2 from the venom of Agkistrodon piscivorus in Escherichia coli: recovery and renaturation from bacterial inclusion bodies. Protein Expres. Purif. 3, 512-517.
13. McPheeters, D.S., Christenson, A., Young, E.T., Stormo, G., Gold, L., 1986. Translational regulation of expression of the bacteriophage T4 lysozyme gene. Nucl. Acids. Res. 14, 5813-5826.
14. Mayford, M., Weisblum, B., 1985. Messenger RNA from Staphylococcus aureus that specifies macrolide-lincosamide streptogramin resistance. Demonstration of its confirmations and of the leader peptide it encodes. J. Mol. Biol. 185, 769-780.
15. Monath, T.P., 1986. Pathobiology of the flaviviruses. In: Schlesinger, S., Schlesinger, M.J. (Eds.), The Togaviridae and Flaviviridae. Plenum Press, New York, pp. 375-440.
16. Sambrook, J., Fritsch, E.F., Maniatis, T., 1989. Molecular Cloning. A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
17. Sanger, F., Nicklen, S., Coulson, A.R., 1977. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
18. Schmidt, B.F., Berkhout, B., Overbeek, G.P., van Strien, A., van Duin, J., 1987. Determination of the RNA secondary structure that regulates lysis gene expression in bacteriophage MS2. J. Mol. Biol. 195, 505-516.
19. Shine, J., Dalgarno, L., 1974. The 3′-terminal sequence of E. coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71, 1342-1346.
20. de Smit, M.H., van Duin, J., 1990. Secondary structure of the ribosome binding site determines translational efficiency: A quantitative analysis. Proc. Natl. Acad. Sci. USA. 87, 7668-7672.
21. de Smit, M.H., van Duin, J., 1994. Control of translation by mRNA secondary structure in E. coli. A quantitative analysis of literature data. J. Mol. Biol. 244, 144-150.
22. Spanjaard, R.A., van Duin, J., 1989. Expression of the rat interferon α-1 gene in Escherichia coli controlled by the secondary structure of the translation-initiation region. Nucleic Acids Res. 17, 5501-5507.
23. Steitz, J.A., 1969. Polypeptide chain initiation: nucleotide sequence of the three ribosomal binding sites in bacteriophage R17 DNA. Nature 224, 957-964.
24. Stormo, G.D., 1986. Translation initiation. In: Reznikoff, W., Gold, L.M. (Eds.). Maximizing Gene Expression. Butterworth, Stoneham, MA, pp. 195-224.
25. Studier, F.W., Rosenberg, A.H., Dunn, J.J., Dubendorff, J.W., 1990. Use of T7 RNA polymerase to direct expression of cloned genes. In: Goeddel, D.V. (Ed.), Methods in Enzymology. Gene Expression Technology. Academic Press, San Diego, Vol. 185, pp. 60-89.
26. Tsunasawa, S., Stewart, J.W., Sherman, F., 1985. Amino terminal processing of mutant forms of yeast iso-1-cytochrome C. The specifities of methionine aminopeptidase and acetyl transferase. J. Biol. Chem. 260, 5382-5391.
27. Wulczyn, F.G., Kahmann, R., 1991. Translational stimulation: RNA sequence and structure requirements for binding of Com protein. Cell 65, 259-269.
28. Yanofsky, C., 1981. Attenuation in the control of expression of bacterial operons. Nature (London) 289, 751-758.
29. Zuker, M., Stiegler, P., 1981. Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information. Nucleic Acids Res. 9, 133-148.