Summary
A three dimensional model is presented which shows the spatial arrangement of 20 of the 21 proteins of the 30S ribosomal subunit ofEscherichia coli. The model fulfills several purposes: (a) It summarizes currently available structural and functional data on ribosomal proteins; (b) It suggests an interesting correlation between stoichiometry and function. Functional proteins are both clustered and fractional; (c) It can be evaluated in relation to new data, and it may predict relationships or point out critical experiments by which it can be tested.
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H. G. Wittmann, G. Stöffler, I. Hindennach, C. G. Kurland, L. Randall-Hazelbauer, E. A. Birge, M. Nomura, E. Kaltschmidt, S. Mizushima, R. R. Traut and T. A. Bickle, Mol. Gen. Genet. 111, 327–333 (1971).
R. R. Traut, C. Ahmad-Zadeh, T. A. Bickle, P. Pearson and A. Tissieres, Cold Spring Harbor Symposium on Quantitative Biology 34, 25–38 (1969).
P. Voynow and C. G. Kurland, Biochemistry 10, 517–523 (1971).
H. J. Weber, Mol. Gen. Genet. 119, 233–248 (1972).
W. E. Hill, J. D. Thompson and J. W. Anderegg, J. Mol. Biol. 44, 89–102 (1969).
G. Stöffler, R. Hasenbank, M. Lütgehaus, R. Maschler, C. A. Morrison, H. Zeichardt and R. A. Garret, Mol. Gen. Genet. 127, 89–110 (1973).
L. P. Visentin, M. Yaguchi and H. Kaplan, Can. J. Biochem. 51, 1487–1497 (1973).
G. Moore and R. R. Crichton, FEBS Letters 37, 74–78 (1973).
R. R. Crichton and H. G. Wittmann, Mol. Gen. Genet. 114, 95–105 (1971).
T. T. Sun, A. Bollen, L. Kahan and R. R. Traut, Biochemistry 13, 2334–2340 (1974).
L. C. Lutter, H. Zeichhardt, C. G. Kurland and G. Stöffler, Mol. Gen. Genet. 119, 357–366 (1972).
L. C. Lutter, U. Bode, C. G. Kurland and G. Stöffler, 129, 167–176 (1974).
F. N. Chang and J. G. Flaks, J. Mol. Biol. 68, 177–180 (1972).
C. T. Shih and G. R. Craven, J. Mol. Biol. 78, 651–663 (1973).
W. Held, B. Ballou, S. Mizushima and M. Nomura, J. Biol. Chem., in the press (1974).
G. R. Craven, The Ribosome (A. Tissieres, M. Nomura, P. Lengyel, eds.) Cold Spring Harbor Laboratory, New York, in the press (1974).
K. H. Nierhaus, K. Bordasch and H. E. Homann, J. Mol. Biol. 74, 587–597 (1973).
W. A. Held and M. Nomura, Biochemistry 12, 3273–3281 (1973).
J. Morgan and R. Brimacombe, Eur. J. Biochem. 37, 472–480 (1973).
P. Schendel, P. Maeba and G. R. Craven, Proc. Natl. Acad. Sci. U.S.A. 69, 544–548 (1972).
H. E. Roth and K. H. Nierhaus, FEBS Letters 31, 35–38 (1973).
R. A. Zimmerman, The Ribosome (A. Tissieres, M. Nomura, P. Lengyel, eds.) Cold Spring Harbor Laboratory, New York, in the press (1974).
H. E. Homann and K. H. Nierhaus, Eur. J. Biochem. 20, 249–257 (1971).
S. Mizushima and M. Nomura, Nature 226, 1214–1218 (1970).
M. Nomura and W. Held, The Ribosome (A. Tissieres, M. Nomura, P. Lengyel, eds.) Cold Spring Harbor Laboratory, New York, in the press (1974).
R. R. Traut, R. L. Heimark, T. T. Sun, A. Bollen and J. W. B. Hershey, The Ribosome (A. Tissieres, M. Nomura, P. Lengyel, eds.) Cold Spring Harbor Laboratory, New York, in the press (1974).
A. Niveleau and D. A. Hawley, Fed. Proc. 33, 1285 Abst. (1974).
C. Gualerzi and C. L. Pon, Biochem. Biophys. Res. Comm. 52, 792–799 (1973).
I. Ginzburg, R. Miskin and A. Zamir, J. Mol. Biol. 79, 481–494 (1973).
D. P. Rummel and H. F. Noller, Nature New Biology 245, 72–75 (1973).
L. L. Randall-Hazelbauer and C. G. Kurland, Mol. Gen. Genet. 115, 234–242 (1972).
P. Traub, K. Hosokawa, G. R. Cragen and M. Nomura, Proc. Nat. Acad. Sci. U.S.A. 58, 2430–2436 (1967).
J. C. Lelong, D. Gros, F. Gros, A. Bollen, Maschler and G. Stöffler, Proc. Nat. Acad. Sci. U.S.A. 71, 248–252 (1974).
M. Nomura, S. Mizushima, M. Osaki, P. Traub and C. V. Lowry, Cold Spring Harbor Symposium on Quantitative Biology 34, 49–61 (1969).
W. A. Held, M. Nomura and J. W. B. Hershey, Mol. Gen. Genet. 128, 11–22 (1974).
H. F. Noller, C. Chang, G. Thomas and J. Aldridge, J. Mol. Biol. 61, 669–679 (1971).
A. Seetharama and P. B. Moore, J. Mol. Biol. 76, 207–221 (1973).
P. H. Van Knippenberg and J. Van Duin, J. Mol. Biol. 84, 185–195 (1974).
J. H. Highland, E. Ochsner, J. Gordon, J. Bodley, R. Hasenbank and G. Stöffler, Proc. Nat. Acad. Sci. U.S.A. 71, 627–630 (1974).
R. C. Marsh and A. Parmeggiani, Proc. Nat. Acad. Sci. U.S.A. 70, 151–155 (1973).
T. T. Sun, L. Kahan and R. R. Traut, J. Mol. Biol., 87, 509–522 (1974).
K. H. Huang and C. R. Cantor, J. Mol. Biol. 67, 265–275 (1972).
R. V. Miller and P. S. Sypherd, J. Mol. Biol. 78, 539–550 (1973).
F. N. Chang, J. Mol. Biol. 78, 563–568 (1973).
C. A. Morrison, R. A. Garret, H. Zeichhardt and G. Stöffler, Mol. Gen. Genet. 127, 359–368 (1974).
G. Schreiner and K. H. Nierhaus, J. Mol. Biol. 81, 71–82 (1973).
O. Pongs and V. A. Erdmann, FEBS Letters 37, 47–50 (1973).
F. N. Chang and J. G. Flaks, Proc. Nat. Acad. Sci. U.S.A. 67, 1321–1328 (1970).
E. Deusser, Mol. Gen. Genet. 119, 249–258 (1972).
E. Deusser and K. H. Nierhaus, Nature 238, 269–270 (1972).
G. W. Tischendorf, G. Stöffler and H. G. Wittmann, Mol. Gen. Genet., in the press (1973).
T. A. Bickle, J. W. B. Hershey and R. R. Traut, Proc. Nat. Acad. Sci. U.S.A. 69, 1327–1331 (1972).
A. Zamir, R. Miskin and D. Elson, J. Mol. Biol. 60, 347–364 (1971).
K. E. Van Holde and W. E. Hill, The Ribosome (A. Tissieres, M. Nomura, P. Lengyel, eds.) Cold Spring Harbor Laboratory, New York, in the press (1974).
D. H. Sachs, A. N. Schechter, A. Eastlake and C. B. Anfinsen, Proc. Nat. Acad. Sci. U.S.A. 69, 3790–3794 (1972).
J. L. Fakunding and J. W. B. Hershey, J. Biol. Chem. 248, 4206–4212 (1973).
S. Sabol and S. Ochoa, Nature New Biology 234, 233–236 (1971).
C. L. Pon, S. M. Friedman and C. Gualerzi, Mol. Gen. Genet. 116, 192–198 (1972).
R. A. Garrett and H. G. Wittmann, Protein Synthesis in Reproductive Tissue (E. Diazlabusy, ed.) Sixth Karolinsky Symposium, pp. 75–91, Karolinsky Institute, Stockholm (1973).
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Sun, TT., Heimark, R.L. & Traut, R.R. The protein topography of the E. coli 30S ribosomal subunit: A preliminary model E. coli/30S subunit/ribosome/spatial arrangement of proteins. Mol Cell Biochem 6, 33–41 (1975). https://doi.org/10.1007/BF01731864
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DOI: https://doi.org/10.1007/BF01731864