Ribosomal protein S7: A new RNA-binding motif with structural similarities to a DNA architectural factor

Harumi Hosaka, Atsushi Nakagawa, Isao Tanaka, Nao Harada, Kazunari Sano, Makoto Kimura, Min Yao, Soichi Wakatsuki

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Background: The ribosome is a ribonucleoprotein complex which performs the crucial function of protein biosynthesis. Its role is to decode mRNAs within the cell and to synthesize the corresponding proteins. Ribosomal protein S7 is located at the head of the small (30S) subunit of the ribosome and faces into the decoding centre. S7 is one of the primary 16S rRNA-binding proteins responsible for initiating the assembly of the head of the 30S subunit. In addition, S7 has been shown to be the major protein component to cross-rink with tRNA molecules bound at both the aminoacyl-tRNA (A) and peptidyl-tRNA (P) sites of the ribosome. The ribosomal protein S7 clearly plays an important role in ribosome function. It was hoped that an atomic-resolution structure of this protein would aid our understanding of ribosomal mechanisms. Results: The structure of ribosomal protein S7 from Bacillus stearothermophilus has been solved at 2.5 Å resolution using multiwavelength anomalous diffraction and selenomethionyl-substituted proteins. The molecule consists of a helical hydrophobic core domain and a β-ribbon arm extending from the hydrophobic core. The helical core domain is composed of a pair of entangled helix-turn-helix motifs; the fold of the core is similar to that of a DNA architectural factor. Highly conserved basic and aromatic residues are clustered on one face of the S7 molecule and create a 168 rRNA contact surface. Conclusions: The molecular structure of S7, together with the results of previous cross-linking experiments, suggest how this ribosomal protein binds to the 3' major domain of 16S rRNA and mediates the folding of 16S rRNA to create the ribosome decoding centre.

Original languageEnglish
Pages (from-to)1199-1208
Number of pages10
JournalStructure
Volume5
Issue number9
DOIs
Publication statusPublished - Sep 15 1997

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ethyl-2-methylthio-4-methyl-5-pyrimidine carboxylate
Ribosomes
DNA
Transfer RNA
Proteins
Helix-Turn-Helix Motifs
Small Ribosome Subunits
Geobacillus stearothermophilus
Ribonucleoproteins
Ribosomal Proteins
Protein Biosynthesis
Molecular Structure
Carrier Proteins
Arm
Head
Messenger RNA
ribosomal protein S7
RNA-Binding Motifs

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

Hosaka, H., Nakagawa, A., Tanaka, I., Harada, N., Sano, K., Kimura, M., ... Wakatsuki, S. (1997). Ribosomal protein S7: A new RNA-binding motif with structural similarities to a DNA architectural factor. Structure, 5(9), 1199-1208. https://doi.org/10.1016/S0969-2126(97)00270-0

Ribosomal protein S7 : A new RNA-binding motif with structural similarities to a DNA architectural factor. / Hosaka, Harumi; Nakagawa, Atsushi; Tanaka, Isao; Harada, Nao; Sano, Kazunari; Kimura, Makoto; Yao, Min; Wakatsuki, Soichi.

In: Structure, Vol. 5, No. 9, 15.09.1997, p. 1199-1208.

Research output: Contribution to journalArticle

Hosaka, H, Nakagawa, A, Tanaka, I, Harada, N, Sano, K, Kimura, M, Yao, M & Wakatsuki, S 1997, 'Ribosomal protein S7: A new RNA-binding motif with structural similarities to a DNA architectural factor', Structure, vol. 5, no. 9, pp. 1199-1208. https://doi.org/10.1016/S0969-2126(97)00270-0
Hosaka, Harumi ; Nakagawa, Atsushi ; Tanaka, Isao ; Harada, Nao ; Sano, Kazunari ; Kimura, Makoto ; Yao, Min ; Wakatsuki, Soichi. / Ribosomal protein S7 : A new RNA-binding motif with structural similarities to a DNA architectural factor. In: Structure. 1997 ; Vol. 5, No. 9. pp. 1199-1208.
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