Abstract
Evidence continues to mount that RNA plays many vital structural and functional roles of the ribosome in protein synthesis (for a review see Thompson and Hearst, 1983 a). Indeed, the recent discovery of catalytic RNA (Kruger et al., 1982; Guerrier-Takada et al., 1983) even raises the possibility that the peptidyl transferase and translocation activities of the ribosome could reside in RNA. For these reasons, it remains vitally important that the structure of the various RNAs that participate in protein synthesis be defined more completely. At present, detailed three-dimensional structure information is available for only one such RNA type, several classes of tRNA. Prospects for obtaining comparable information on the free 5S prokaryotic rRNA appear good. However, much less is known about the structures of these RNAs as they participate in protein synthesis on the ribosome. We have only secondary structure information for the larger ribosomal RNAs and for mRNAs. Most of this information is restricted to the free RNA. Studies on the ribosome-bound species are much more difficult to interpret unequivocally because many techniques really cannot distinguish well between direct information on RNA structure and information about RNA-protein contacts.
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References
Castles, J.J., Singer, M.F. (1969). Degradation of polyuridylic acid by ribonuclease II: protection by ribosomes. J. Mol. Biol. 40: 1–17.
Chatterjee, P.K., Cantor, C.R. (1978). Photochemical production of psoralen-DNA monoadducts capable of subsequent photocrosslinking. Nucl. Acids Res. 5: 36
Chu, Y.G., Wollenzien, P.L., Cantor, C.R. (1983). Use of psoralen monoadducts to compare the structure of 16S rRNA in active and inactive 30S ribosomal subunits. J. Biomolec. Struct. Dyn. 1: 647–656.
Evstafieva, A., Shatsky, I.N., Bogdanov, A.A., Semenkov, Y., Vasiliev, V.D. (1983). Localization of 5′ and 3′ ends of the ribosome-bound segment of template polynucleotides by immune electron microscopy. EMBO J. 2: 799–804.
Garrett-Wheeler, E., Lockard, R.E., Kumar, A. (1984). Mapping of psoralen cross- linked nucleotides in RNA. Nucl. Acids Res. 12: 3405–3423.
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., Altman, S. (1983). The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35: 849–857.
Hogan, J.J., Noller, H.F. (1978). Altered topography of 16S RNA in the inactive form of E. coli 30S ribosomal subunits. Biochemistry 17: 587–593.
Hui, C.F., Cantor, C.R. (1985). Mapping the location of psoralen crosslinks on RNA by mung bean nuclease (ribosomal RNA/Shine-Dalgarno sequence/RNA secondary structure/nucleotide sequence). Proc. Natl. Acad. Sci. 82: 1381–1385.
Kang, C., Cantor, C.R. (1985a). Enzymatic synthesis of uniformly 32P-labeled polyribonucleotides and high specific activity ribonucleoside 5′ [a-32p] diphosphates. Anal. Biochem. 144: 291–295.
Kang, C., Cantor, C.R. (1985b). Structure of ribosome-bound messenger RNA as revealed by enzymatic accessibility studies. J. Mol. Biol. 181: 241–251.
Kruger, K., Grabowski, P.J., Zaug, A.J., Sands, J., Gottschling, D.E., Cech, T.R. (1982). Self-splicing RNA: autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena. Cell 31: 147–157.
Leng, M., Dourlent, M., Helene, C. (1975). Interactions in nucleic acids. In: Physicochemical properties of nucleic acids. II. Structure and conformation of polynucleotides, ed. Duchesne, J. Academic Press, New York, pp. 32–37.
Pochon, F., Amand, B., Lavalette, D. (1977). Rotational diffusion of E. coli ribosomes II. Ribosome attachment to polyuridylic acid. Biochimie 59: 785–788.
Prince, J.B., Taylor, B.H., Thurlow, D.L., Ofengand, J., Zimmerman, R.A. (1982). Covalent crosslinking of tRNA1 Val to 16S RNA at the ribosomal P site; identification of crosslinked residues. Proc. Natl. Acad. Sci. USA 79: 5450–5454.
Quarless, S., Cantor, C.R. (1985). Analysis of RNA structure by UV crosslinking and denaturation gel electrophoresis. Anal. Biochem. 147, 296–300.
Steiner, R., Millar, D.B. (1970). The nucleic acids. In: Biological polyelectrolytes, ed. Veis, A. Marcel Dekker, New York, pp. 65–130.
Steitz, J.A. (1979). Ribosomes. Structure, function and genetics, ed. Chambliss, G. et al. University Park Press, Baltimore, pp. 479–495.
Takanami, M., Zubay, G. (1964). An estimate of the size of the ribosomal site for messenger RNA binding. Proc. Natl. Acad. Sci. USA 51: 834–838.
Thammana, P., Cantor, C.R., Wollenzien, P.L., Hearst, J.E. (1979). Crosslinking studies of the organization of the 16S ribosomal RNA within the 30S E. coli ribosomal subunit. J. Mol. Biol. 135: 271–283.
Thompson, J.F., Hearst, J.E. (1983a). Structure-function relations in E. coli 16S RNA. Cell 33: 19–24.
Thompson, J.F., Hearst, J.E. (1983b). Structure of E. coli 16S RNA elucidated by psoralen crosslinking. Cell 32: 1353–1365.
Woese, C.R., Gutell, R., Gupta, R., Noller, H.F. (1983). Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids. Microbiol. Rev. 47: 621–669.
Wollenzien, P.L., Cantor, C.R. (1982a). Marking the polarity of E. coli rRNA molecules for electron microscopy by covalent attachment of psoralen-DNA restriction fragments. Proc. Natl. Acad. Sci. USA 79: 3940–3944.
Wollenzien, P.L., Cantor, C.R. (1982b). A gel electrophoretic technique for separating crosslinked RNAs: application to improved electron microscopic analysis of psoralen crosslinked 16S rRNA. J. Mol. Biol. 159: 151–166.
Wollenzien, P.L., Hearst, J.E., Squires, C., Squires, C. (1979a). Determining the polarity of the map of crosslinked interactions in E. coli 16S ribosomal RNA. J. Mol. Biol. 135:285–291.
Wollenzien, P.L., Hearst, J.E., Thammana, P., Cantor, C.R. (1979b). Base pairing between distant regions of the E. coli 16S in solution. J. Mol. Biol. 135: 255–269.
Wollenzien, P.L., Murphy, R.F., Cantor, C.R., Expert-Bezason, A., Hayes, D. (1985). Structure of the E. coli 16S rRNA: psoralen crosslinks and N-acetyl-N′-(p- glyoxylylbenzoyl) cystamine crosslinks detected by electron microscopy. J. Mol. Biol. 184: 67–80.
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Cantor, C.R., Hui, CF., Kang, C., Smith, C.L., Wollenzien, P.L. (1986). RNA Structure in Solution and on the 30S Ribosomal Subunit. In: Hardesty, B., Kramer, G. (eds) Structure, Function, and Genetics of Ribosomes. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4884-2_12
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DOI: https://doi.org/10.1007/978-1-4612-4884-2_12
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