Skip to main content
Log in

mRNP proteins, initiation factors and phosphorylation

  • Published:
Molecular Biology Reports Aims and scope Submit manuscript

Abstract

Information has been collected to stimulate interest regarding the nature and the possible role of mRNP protein phosphorylation in a cytoplasmic control mechanism for protein synthesis. It does not imply a direct relationship between mRNP protein and initiation factors. These proteins have some properties in common (e.g. molecular weight, phosphorylation, protein kinase, mRNA binding activity). We emphasize that some free mRNP may be translatable after modification of their protein by interference factors belonging to other cellular compartments. Thus, some mRNP proteins might possess initiation factor or protein synthetic activity if we accept Spirin's theory, i.e., “Eukaryotic messenger RNA and informosomes omnia mea mecum porto”

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Spirin, A.S., Eur. J. Biochem. 10, 20–35 (1969).

    Google Scholar 

  2. Van Venrooij W.J., Janssen Dick B., Mol. Biol. Rep. 4, 1: 3–8 (1978).

    Google Scholar 

  3. Preobrazhensky A.A., Spirin A.S., Progress in Nucleic Acid Research and Molecular Biology 21, 2–38 (1978).

    Google Scholar 

  4. Egly J.M., Stevenin J., Path. Biol. 25, no 10, 741–754 (1977).

    Google Scholar 

  5. Perry R.P., Kelley D.E., J. Mol. Biol. 35, 37–59 (1968).

    Google Scholar 

  6. Spohr G., Granboulan N., Morel C., Scherrer K., Eur. J. Biochem. 17, 296–318 (1970).

    Google Scholar 

  7. Sugano H., Suda S., Kawada T., Sugano I., Biochim. Biophys. Acta 238, 139–149 (1971).

    Google Scholar 

  8. Gander E.S., Stewart A.G., Morel C., Scherrer K., Eur. J. Biochem. 38, 443–452 (1973).

    Google Scholar 

  9. Soeiro R., Vaughan M.H., Warner J.R., Darnell J.E., J. Cell Biol. 39, 112–118 (1968).

    Google Scholar 

  10. Brandhort B., McConkey E., J. Mol. Biol. 85, 451–463 (1974).

    Google Scholar 

  11. Buckingham M.E., Caput D., Cohen A., Whalen R.G., Gros F., Proc. Nat. Acad. Sci. US 71, 1466–1470 (1974).

    Google Scholar 

  12. Iatrou K., Dixon G.H., Cell 10, 433–441 (1977).

    Google Scholar 

  13. Gross K.W., Jacobs-Lorena M., Baglioni C., Gross P.R., Proc. Nat. Acad. Sci. US 70, 9, 2614–2618 (1973).

    Google Scholar 

  14. Zahringer J., Baliga B.S., Munro H.N., Proc. Nat. Acad. Sci. 73, 857–881 (1976).

    Google Scholar 

  15. Houdebine L.M., Delouis C., Devinoy E., Biochimie 60, 809–812 (1978).

    Google Scholar 

  16. Enger M.D., Campbell E.W., Hanners J.L., Febs. Lett. 55, 194–197 (1975).

    Google Scholar 

  17. Mac Leod C., Biochemistry 14, 4011–4018 (1975).

    Google Scholar 

  18. Freienstein C., Blobel G., Proc. Nat. Acad. Sci. US 71, 3435–3439 (1974).

    Google Scholar 

  19. Ernst V., Arnstein H.R.V., Biochim. Biophys. Acta 378, 251–259 (1975).

    Google Scholar 

  20. Chen J.H., Lavers G.C., Spector A., Biochim. Biophys. Acta 418, 39–51 (1976).

    Google Scholar 

  21. Spohr G., Kayibanda B., Scherrer K., Eur. J. Biochem. 31, 194–208 (1972).

    Google Scholar 

  22. Bag J., Sarkar S., Biochemistry 14, 3800–3807 (1975).

    Google Scholar 

  23. Bag J., Sarkar S., J. Biol. Chem. 251, 7600–7609 (1976).

    Google Scholar 

  24. Civelli O., Vincent A., Buri J.F., Scherrer K., Febs. Lett. 72, 71–76 (1976).

    Google Scholar 

  25. Shafritz D.A., J. Biol. Chem. 249, 81–88 (1974).

    Google Scholar 

  26. Huang A.S., Baltimore D., J. Mol. Biol. 47, 275–291 (1970).

    Google Scholar 

  27. Olsnes S., Eur. J. Biochem. 18, 242–249 (1971).

    Google Scholar 

  28. Kempf J., Egly J.M., Stricker Ch., Schmitt M., Mandel P., Febs. Lett. 26, 1 130–134 (1972).

    Google Scholar 

  29. Lindberg U., Sundquist B., J. Mol. Biol. 86, 451–468 (1974).

    Google Scholar 

  30. Gander E.S., Mueller R.U., Goldenberg S., Morel C., Mol. Biol. Rep. 2, 343–346 (1975).

    Google Scholar 

  31. Liautard J.P., Setyono B., Spindler E., Köhler K., Biochim. Biophys. Acta 425, 373–383 (1976).

    Google Scholar 

  32. Van der Marel, Tasseron de Jong J. G., Bosch L., Febs. Lett. 51, 330–334 (1975).

    Google Scholar 

  33. Auerbach S., Pederson Th. Biochem. Biophys. Res. Commun. 63, 149–156 (1975).

    Google Scholar 

  34. Hellermann J.G., Shafritz D.A., Proc. Nat. Acad. Sci. US 72, 3, 1021–1025 (1975).

    Google Scholar 

  35. Barrieux A., Ingraham H.A., David D.N., Rosenfeld M.G., Biochemistry 14, 1815–1821 (1975).

    Google Scholar 

  36. Mizushima S., Nomura M., Nature 226, 1214–1219 (1970).

    Google Scholar 

  37. Zawislak R., Stevenin J., Jacob M., Biochimie 56, 91–98 (1974).

    Google Scholar 

  38. Egly J.M., Krieger O., Mandel P., Kempf J., Febs. Lett. 40, 101–105 (1974).

    Google Scholar 

  39. Globel G., Proc. Nat. Acad. Sci. US 70, 924–928 (1973).

    Google Scholar 

  40. Gander E.S., Stewart A.G., Morel C., Scherrer K., Eur. J. Biochem. 38, 443–452 (1973).

    Google Scholar 

  41. Egly J.M., Johnson B.C., Stricker Ch. Mandel P., Kempf J., Febs. Lett. 22 181–184 (1972).

    Google Scholar 

  42. Schmitt M., Egly J.M., Mandel P., Kempf J., Biochimie 55, 653–659 (1973).

    Google Scholar 

  43. Quirin-Stricker Ch., Schmitt M., Egly J.M., Kempf J., Eur. J. Biochem. 62, 199–209 (1978).

    Google Scholar 

  44. Quirin-Stricker Ch., Schmitt M., personal communication.

  45. Egly J.M., Elkaim R., Kempf J., submitted for publication.

  46. Liautard J.P., Personal communication.

  47. Schmitt M., Kempf J., Quirin-Stricker Ch., Biochim. Biophys. Acta 481, 438–449 (1977).

    Google Scholar 

  48. Cenatiempo Y., Genot A., Cozzone A.J., Reboud J.P., Biochimie 60, 813–816 (1978).

    Google Scholar 

  49. Fan H., Penman S., J. Mol. Biol. 50, 655–670 (1970).

    Google Scholar 

  50. Pain V.M., Clemens M.J., Febs. Lett. 32, 205–212 (1973).

    Google Scholar 

  51. Palmiter R.D., Cell 4, 189–197 (1975).

    Google Scholar 

  52. Weissbach H., Ochoa L., Ann. Rev. Biochem. 45, 191–216 (1976).

    Google Scholar 

  53. Revel M., Molecular Mechanisms of Protein Biosynthesis 245–321 (1977) Acad. P.N.

  54. Benne R., Hershey J.W.B., Proc. Nat. Acad. Sci. US 73, 3005–3009 (1976).

    Google Scholar 

  55. Benne R., Wong C., Luedi M., Hershey J.W.B., J. Biol. Chem. 251, 7675–7681 (1976).

    Google Scholar 

  56. Benne R., Luedi M.L., Hershey J.W.B. J. Biol. Chem. 252, 5798–5803 (1977).

    Google Scholar 

  57. Benne R., Brown Luedi M.L., Hershey J.W.B., J. Biol. Chem. 253, 3070–3077 (1978)

    Google Scholar 

  58. Schreier M.H., Erni B., Staehelin T., J. Mol. Biol. 116, 727–753 (1977).

    Google Scholar 

  59. Staehelin T., Trachsel H., Erni B., Boschetti A., Schreier M.H., Febs. Proc. Meet 10, 309–323 (1975).

    Google Scholar 

  60. Safer B., Anderson W.F., Merrick W.C., J. Biol. Chem. 250, 9067–9075 (1975).

    Google Scholar 

  61. Merrick W.C., Kemper W.M., Anderson W.F., Proc. Nat. Acad. Sci. US 72, 5556–5562 (1975).

    Google Scholar 

  62. Prichard P.M., Anderson W.F., Methods Enzymol. 30, 136–141 (1974).

    Google Scholar 

  63. Safer B., Adams S.L., Kemper W.M., Berry K.W., Lloyd M., Merrick W.C., Proc. Nat. Acad. Sci. US 73, 2584–2588 (1976).

    Google Scholar 

  64. Kemper W.M., Berry K.W., Merrick W.C., J. Biol. Chem. 251, 5551–5557 (1976).

    Google Scholar 

  65. Benne R., Edman J., Traut R.R., Hershey J.W.B., Proc. Nat. Acad. Sci. US 75, 108–112 (1978).

    Google Scholar 

  66. Traugh J.A., Tahara S.M., Sharp S.B., Safer B., Merrick W.C., Nature 263, 163–165 (1976).

    Google Scholar 

  67. Issinger O.G., Benne R., Hershey J.W.B., Trau R.R., J. Biol. Chem. 251, 6471–6474 (1976).

    Google Scholar 

  68. Levin D.H., Ranu R.S., Ernst V., London I.M., Proc. Nat. Acad. Sci. US 73, 3112–3116 (1976).

    Google Scholar 

  69. Kramer G., Cimadevilla M.J. Hardesty B., Proc. Nat. Acad. Sci. US 73, 3078–3082 (1978).

    Google Scholar 

  70. Farrell P.J., Balkow K., Hunt T., Jackson R.J., Cell 11, 187–200 (1977).

    Google Scholar 

  71. Ranu R.S., London I.M., Das A., Dasgupta A., Majumdar A., Ralston R., Roy R., Gupta N.K., Proc. Nat. Acad. Sci. US 75, 745–749 (1978).

    Google Scholar 

  72. Maxwell C.R., Kamper C.S., Rabinovitz M., J. Mol. Biol. 58, 317–327 (1971).

    Google Scholar 

  73. Farrell P.J., Hunt T., Jackson R.J., Eur. J. Biochem. 89, 517–521 (1978).

    Google Scholar 

  74. Datta A., De Haro C., Sierra J.M., Ochoa L., Proc. Nat. Acad. Sci. US 74, 1463–1467 (1977).

    Google Scholar 

  75. Pierre M., Loeb J.E., Biochem. Biophys. Res. Commun. 77, 481–488 (1977).

    Google Scholar 

  76. Zilberstein A., Federman P., Shulman L., Revel M., Febs Lett. 68, 119–124 (1976).

    Google Scholar 

  77. Lebleu B., Sen G.C., Shaila S., Cabrer B., Lengyel P., Proc. Nat. Acad. Sci. US 73, 3107–3111 (1976).

    Google Scholar 

  78. Roberts W.K., Hovanessian A., Brown R.E., Clemens M.J., Kerr I.M., Nature 264, 477–480 (1976).

    Google Scholar 

  79. Pinphanichakarn P., Kramer G., Hardesty B., J. Biol. Chem. 252, 2106–2112 (1977).

    Google Scholar 

  80. Benne R., Hershey J.W.B., J. Biol. Chem. 253, 3078–3087 (1978).

    Google Scholar 

  81. Golini F., Thach S.S., Birge C.H., Safer B., Merrick W.C., Thach R.E., Proc. Nat. Acad. Sci. US 73, 3040–3044 (1976).

    Google Scholar 

  82. Kabat D., Chappel M.R., J. Biol. Chem. 252, 2684–2690 (1977).

    Google Scholar 

  83. Shafritz D.A., Weinstein J.A., Safer B., Merrick W.C., Weber L.A., Hickey E.D., Baglioni C., Nature 261, 291–294 (1976).

    Google Scholar 

  84. Merrick W.C., Peterson D.T., Safer B., Lloyd M., Kemper W.M., Febs Meeting Gene Expression, Clark Br., Klenow M. Eds, Pergamon Press Vol. 43, 17–27 (1977).

  85. Pahlmann S., Rosengren J., Hjerten S., J. Chromatogr. 131, 99–108 (1977).

    Google Scholar 

  86. Shafritz D.A., Molecular Mechanisms of Protein Biosynthesis (Weisbach M. Pelska S. Eds, Academic Press (1977)).

  87. Lingrel J.B., Lockard R.E., Jones R.F., Burr H.E., Holder J.W., Ser Haematal 4, 3–10 (1971).

    Google Scholar 

  88. Sampson J., Mathews M.B., Osborn M., Borghetti A.F., Biochemistry 11, 3636–3640 (1972).

    Google Scholar 

  89. Hendrick D., Schwarz W., Pitzel S., Tiedemann H. Biochim. Biophys. Acta 340 278–284 (1974).

    Google Scholar 

  90. Cashion L.M., Stanley W.M. Jr., Proc. Nat. Acad. Sci US 71, 436–440 (1974).

    Google Scholar 

  91. Barrieux A., Rosenfeld M.A., J. Biol. Chem. 252, 392–398 (1977).

    Google Scholar 

  92. Jergil B., Eur. J. Biochem. 28, 546–554 (1972).

    Google Scholar 

  93. Tao M., Salas M.T., Lipman F., Proc. Nat. Acad. Sci. US 67, 408–414 (1970).

    Google Scholar 

  94. Egly J.M., Schmitt M., Kempf J., Biochim. Biophys. Acta 454, 549–557 (1976).

    Google Scholar 

  95. Quirin Stricker Ch., Schmitt M., Biochim. Biophys. Acta 477, 414–426 (1977).

    Google Scholar 

  96. Rubin Ch.S., Rosen O.M., Annu. Rev. Biochem. 831–887 (1975).

  97. Ovchinnikov L.P., Spirin A.S., Erni B., Stachelin T., Febs Lett. 88, 21–26 (1978).

    Google Scholar 

  98. Miller R.L., Schweet R., Arch. Biochem. Biophys. 125, 632–646 (1968).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Egly, J.M., Elkaim, R. & Pierre, M. mRNP proteins, initiation factors and phosphorylation. Mol Biol Rep 5, 91–97 (1979). https://doi.org/10.1007/BF00777494

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00777494

Keywords

Navigation