Characterization of Moloney murine leukaemia virus/avian myeloblastosis virus chimeric reverse transcriptases

Journal of Biochemistry

Volumn 145, Issue 3, 2009, Pages 315-324

  Yasukawa, Kiyoshi ^a   Mizuno, Masaki ^a   Inouye, Kuniyo ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Avian myeloblastosis virus; Chimeric enzyme; Moloney murine leukaemia virus; Reverse transcriptase; RNase H

Indexed keywords

RNA DIRECTED DNA POLYMERASE; RECOMBINANT PROTEIN; RIBONUCLEASE H;

AMINO ACID SEQUENCE; ARTICLE; AVIAN MYELOBLASTOSIS VIRUS; CRYSTAL STRUCTURE; MOLECULAR WEIGHT; MOLONEY LEUKEMIA ONCOVIRUS; NONHUMAN; NUCLEOTIDE SEQUENCE; REVERSE TRANSCRIPTION; SEQUENCE HOMOLOGY; BIOCATALYSIS; CHEMISTRY; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE ALIGNMENT; TEMPERATURE;

AVIAN MYELOBLASTOSIS VIRUS; MURINAE;

AMINO ACID SEQUENCE; AVIAN MYELOBLASTOSIS VIRUS; BIOCATALYSIS; CLONING, MOLECULAR; ELECTROPHORESIS, POLYACRYLAMIDE GEL; KINETICS; MOLECULAR SEQUENCE DATA; MOLONEY MURINE LEUKEMIA VIRUS; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTION; RIBONUCLEASE H; RNA-DIRECTED DNA POLYMERASE; SEQUENCE ALIGNMENT; TEMPERATURE;

EID: 66549090946     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn166     Document Type: Article

References (44)

1. Temin, H.M. and Mizutani, S. (1970) RNA-dependent DNA polymerase in virions of Rous sarcoma virus. Nature 226, 1211-1213
2. Baltimore, D. (1970) RNA-dependent DNA polymerase in virions of RNA tumour viruses. Nature 226, 1209-1211
3. Kimmel, A.R. and Berger, S.L. (1987) Preparation of cDNA and the generation of cDNA libraries: overview. Methods Enz. 152, 307-316
4. Kievits, T., van Gemen, B., van Strijp, D., Schkkink, P., Dircks, M., Adriaanse, H., Malek, L., Sooknanan, R., and Lens, P. (1991) NASBA isothermal enzymatic in vitro nucleic acid amplification optimized for the diagnosis of HIV-1 infection. J. Virol. Methods 35, 273-286
5. Ishiguro, T., Saitoh, J., Horie, R., Hayashi, T., Ishizuka, T., Tsuchiya, S., Yasukawa, K., Kido, T., Nakaguchi, Y., Nishibuchi, M., and Ueda, K. (2003) Intercalation activating fluorescence DNA probe and its application to homogeneous quantification of a target sequence by isothermal sequence amplification in a closed vessel. Anal. Biochem. 314, 77-86
6. Masuda, N., Yasukawa, K., Isawa, Y., Horie, R., Saito, J., Ishiguro, T., Nakaguchi, Y., Nishibuchi, M., and Hayashi, T. (2004) Rapid detection of tdh and trh mRNAs of Vibrio parahaemolyticus by the transcription-reverse transcription concerted (TRC) method. J. Biosci. Bioeng. 98, 236-243
7. Roberts, J.D., Bebenek, K., and Kunkel, T.A. (1988) The accuracy of reverse transcriptase from HIV-1. Science 242, 1171-1173
8. Georgiadis, M.M., Jessen, S.M., Ogata, C.M., Telesnitsky, A., Goff, S.P., and Hendrickson, W.A. (1995) Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase. Structure 3, 879-892
9. Das, D. and Georgiadis, M.M. (2004) The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus. Structure 12, 819-829 (Pubitemid 38595770)
10. Lim, D., Gregorio, G.G., Bingman, C., Martinez-Hackert, E., Hendrickson, W.A., and Goff, S.P. (2006) Crystal structure of the Moloney murine leukemia virus RNaseH domain. J. Virol. 80, 8379-8389 (Pubitemid 44384851)
11. Khlstaedt, L.A., Wang, J., Friedman, J.M., Rice, P.A., and Steitz, T.A. (1992) Crystal structure at 3.5Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256, 1783-1790
12. Bieth, E. and Darlix, J.-L. (1991) Complete nucleotide sequence of a highly infectious avian leucosis virus. Nucleic Acids Res. 20, 367
13. DeStefano, J.J., Buiser, R.G., Mallaber, L.M., Myers, T.W., Bambara, R.A., and Fay, P.J. (1991) Polymerization and RNase H activities of reverse transcriptases from Avian myeloblastosis, human immunodeficiency, and Moloney murine leukemia viruses are functionally uncoupled. J. Biol. Chem. 266, 7423-7431
14. Chowdhury, K., Kaushik, N., Pandey, V.N., and Modak, M.J. (1996) Elucidation of the role of Arg110 of murine leukemia virus reverse transcriptase in the catalytic mechanism: biochemical characterization of its mutant enzymes. Biochemistry 35, 16610-16620 (Pubitemid 27020504)
15. Shi, Q., Singh, K., Srivastaba, A., Kaushik, N., and Modak, M.J. (2002) Lysine 152 of MuLV reverse transcriptase is required for the integrity of the active site. Biochemistry 41, 14831-14842 (Pubitemid 35470661)
16. Werner, S. and Wohrl, B.M. (2000) Asymmetric subunit organization of heterodimeric Rous sarcoma virus reverse transcriptase αβ: localization of the polymerase and RNase H active sites in the α subunit. J. Virol. 74, 4740-4744 (Pubitemid 30143749)
17. Goedken, E.R. and Marqusee, S. (1999) Metal binding and activation of the ribonuclease H domain from Moloney murine leukemia virus. Protein Eng. 12, 975-980
18. Huang, H., Chopra, R., Verdine, G.L., and Harrison, S.C. (1998) Structure of covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282, 1669-1675 (Pubitemid 28549275)
19. Kotewicz, M.L., Sampson, C.M., D'Alessio, J.M., and Gerard, G.F. (1988) Isolation of cloned Moloney murine leukemia virus reverse transcriptase lacking ribonuclease H activity. Nucleic Acids Res. 16, 265-277
20. Gerard, G.F., Schmidt, B.J., Kotewicz, M.L., and Campbell, J.H. (1992) cDNA synthesis by Moloney murine leukemia virus RNase H-minus reverse transcriptase possessing full DNA polymerase activity. Focus 14, 91-93
21. Yasukawa, K., Nemoto, D., and Inouye, K. (2008) Comparison of the thermal stabilities of reverse transcriptases from avian myeloblastosis virus and Moloney murine leukaemia virus. J. Biochem. 143, 261-268 (Pubitemid 351238169)
22. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
23. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
24. Sakoda, M. and Hiromi, K. (1976) Determination of the best-fit values of kinetic parameters of the Michaelis-Menten equation by the method of least squares with Taylor expansion. J. Biochem. 80, 547-555
25. Kotewicz, M.L., D'Alessio, J.M., Driftmier, K.M., Blodgett, K.P., and Gerard, G.F. (1985) Cloning and overexpression of Moloney murine leukemia virus reverse transcriptase in Escherichia coli. Gene 35, 249-258 (Pubitemid 15010787)
26. Tanese, N., Roth, M., and Goff, S.P. (1985) Expression of enzymatically active reverse transcriptase in Escherichia coli. Proc. Natl Acad. Sci. USA 82, 4944-4948
27. Roth, M.J., Tanese, N., and Goff, S.P. (1985) Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coli. J. Biol. Chem. 260, 9326-9335
28. Soltis, D.A. and Skalka, A.M. (1988) The α and β chains of avian retrovirus reverse transcriptase independently expressed in Escherichia coli: characterization of enzymatic activities. Proc. Natl Acad. Sci. USA 85, 3372-3376
29. Werner, S. and Wohrl, B.M. (1999) Soluble Rous sarcoma virus reverse transcriptases a, ab, and b purified from insect cells are processive DNA polymerases that lack an RNase H 3′→5′ directed processing activity. J. Biol. Chem. 374, 26329-26336
30. Sevilya, Z., Loya, S., Adir, N., and Hizi, A. (2003) The ribonuclease H activity of the reverse transcritpases of human immunodeficiency viruses type 1 and type 2 is modulated by residue 294 of the small subunit. Nucleic Acids Res. 31, 1481-1487 (Pubitemid 36304910)
31. Gerard, G.F., Potter, R.J., Smith, M.D., Rosenthal, K., Dhariwal, G., Lee, J., and Chatterjee, D.K. (2002) The role of template-primer in protection of reverse transcriptase from thermal inactivation. Nucleic Acids Res. 30, 3118-3129 (Pubitemid 34846176)
32. Cote, M.L. and Roth, M.J. (2008) Murine leukemia virus reverse transcriptase: structural comparison with HIV-1 reverse transcriptase. Virus Res. 134, 186-202
33. Patel, P.H., Jacobo-Molina, A., Ding, J., Tantillo, C., Clark, A.D., Jr, Raag, R., Nanni, R.G., Hughes, S.H., and Arnold, E. (1995) Insights into DNA polymerization mechanisms from structure and function analysis of HIV-1 reverse transcriptase. Biochemistry 34, 5351-5363
34. Ding, J., Das, K., Hsiou, Y., Sarafianos, S.G., Clark, A.D., Jr, Jacobo-Molina, A., Tantillo, C., Hughes, S.H., and Arnold, E. (1998) Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-strand DNA template-primer and an antibody Fab fragment at 2.8Å resolution. J. Mol. Biol. 284, 1095-1111
35. Pandey, P.K., Kaushik, N., Talele, T.T., Yadav, P.N.S., and Pandey, V.N. (2001) Insertion of a peptide from MuLV RT into the connection subdomain of HIV-1 RT results in a functionally active chimeric enzyme in monomeric conformation. Mol. Cell. Biochem. 225, 135-144
36. Pandey, P.K., Kaushik, N., Singh, K., Sharma, B., Upadhyay, A.K., Kumar, S., Harris, D., and Pandey, V.N. (2002) Insertion of a small peptide of six amino acids into the β7-β8 loop of the p51 subunit of HIV-1 reverse transcriptase perturbs the heterdimer and affects its activities. BMC Biochem. 3, 18 (Pubitemid 38994192)
37. Yasukawa, K., Tsuchiya, S., Ekida, T., Iida, H., Ide, T., Miki, D., Yagame, H., Murayama, K., and Ishiguro, T. (2003) Fusion protein of interleukin-6 and interleukin-6 receptor without polypeptide linker. J. Biosci. Bioeng. 96, 38-46
38. Yutani, K., Ogasahara, K., Tsujita, T., and Sugino, Y. (1987) Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase α subunit. Proc. Natl Acad. Sci. USA 84, 4441-4444
39. Shoichet, B.K., Baase, W.A., Kuroki, R., and Matthews, B.W. (1995) A relationship between protein stability and protein function. Proc. Natl Acad. Sci. USA 92, 452-456
40. Lee, S., Oneda, H., Minoda, M., Tanaka, A., and Inouye, K. (2006) Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis α-amylase and insights into engineering α-amylase variants active under acidic conditions. J. Biochem. 139, 997-1005 (Pubitemid 44196876)
41. Lee, A., Mouri, Y., Minoda, M., Oneda, H., and Inouye, K. (2006) Comparison of the wild-type α-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amylase. J. Biochem. 139, 1007-1015 (Pubitemid 44196877)
42. Yasukawa, K. and Inouye, K. (2007) Improving the activity and stability of thermolysin by site-directed mutagenesis. Biochim. Biophys. Acta 1774, 1281-1288
43. Takita, T., Aono, T., Sakurama, H., Itoh, T., Wada, T., Minoda, M., Yasukawa, K., and Inouye, K. (2008) Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability. Biochim. Biophys. Acta 1784, 481-488
44. Muller, B., Restle, T., Weiss, S., Gautel, M., Sczakiel, G., and Goody, R.S. (1989) Co-expression of the subunits of the heterodimer of HIV-1 reverse transcriptase in Escherichia coli. J. Biol. Chem. 264, 13975-13978