The primary and secondary structure of yeast 26S rRNA (original) (raw)

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Biochemisch Laboratorium, Vrije Universiteit

de Boelelaan 1083, 1081 HV Amsterdam, The Netherlands

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Biochemisch Laboratorium, Vrije Universiteit

de Boelelaan 1083, 1081 HV Amsterdam, The Netherlands

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Biochemisch Laboratorium, Vrije Universiteit

de Boelelaan 1083, 1081 HV Amsterdam, The Netherlands

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Biochemisch Laboratorium, Vrije Universiteit

de Boelelaan 1083, 1081 HV Amsterdam, The Netherlands

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Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., Laboratoire de Biochimie

15, rue R. Descartes, 67084, Strasbourg Cedex, France

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Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., Laboratoire de Biochimie

15, rue R. Descartes, 67084, Strasbourg Cedex, France

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Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., Laboratoire de Biochimie

15, rue R. Descartes, 67084, Strasbourg Cedex, France

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Received:

19 October 1981

Published:

21 December 1981

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Geertruida M. Veldman, Jacobus Klootwijk, Victoria C.H.F. de Regt, Rudi J. Planta, Christiane Branlant, Alain Krol, Jean-Pierre Ebel, The primary and secondary structure of yeast 26S rRNA, Nucleic Acids Research, Volume 9, Issue 24, 21 December 1981, Pages 6935–6952, https://doi.org/10.1093/nar/9.24.6935
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Abstract

We present the sequence of the 26S rRNA of the yeast Saccharomyces carlsbergensis as inferred from the gene sequence. The molecule is 3393 nucleotides long and consists of 48% G+C; 30 of the 43 methyl groups can be located in the sequence. Starting from the recently proposed structure of E. coli 23S rRNA (see ref. 25) we constructed a secondary structure model for yeast 26S rRNA. This structure is composed of 7 domains closed by long-range base pairings as in the bacterial counterpart. Most domains show considerable conservation of the overall structure; unpaired regions show extended sequence homology and the base-paired regions contain many compensating base pair changes. The extra length of the yeast molecule is due to a number of insertions in most of the domains, particularly in domain II. Domain VI, which is extremely conserved, is probably part of the ribosomal A site. α-Sarcin, which apparently inhibits the EF-1 dependent binding of aminoacyl-tRNA, causes a cleavage between position 3025 and 3026 in a conserved loop structure, just outside domain VI. Nearly all of the located methyl groups, like in E. coli, are present in domain II, V and VI and clustered to a certain extent mainly in regions with a strongly conserved primary structure. The only three methyl groups of 26S rRNA which are introduced relatively late during the processing are found in single stranded loops in domain VI very close to positions which have been shown in E. coli 23S rRNA to be at the interface of the ribosome.

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© 1981 IRL Press Limited

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