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STRUCTURAL BIOLOGY

Structural Characterization of the Ribosome Maturation Protein, RimM

Sakura Suzuki, Ayako Tatsuguchi, Eiko Matsumoto, Masahito Kawazoe, Tatsuya Kaminishi, Mikako Shirouzu, Yutaka Muto, Chie Takemoto, Shigeyuki Yokoyama
Sakura Suzuki
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Ayako Tatsuguchi
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Eiko Matsumoto
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Masahito Kawazoe
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Tatsuya Kaminishi
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Mikako Shirouzu
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Yutaka Muto
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Chie Takemoto
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
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Shigeyuki Yokoyama
1RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
2Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
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  • For correspondence: yokoyama@biochem.s.u-tokyo.ac.jp
DOI: 10.1128/JB.00024-07
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ABSTRACT

The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded β-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19.

  • Copyright © 2007 American Society for Microbiology
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Structural Characterization of the Ribosome Maturation Protein, RimM
Sakura Suzuki, Ayako Tatsuguchi, Eiko Matsumoto, Masahito Kawazoe, Tatsuya Kaminishi, Mikako Shirouzu, Yutaka Muto, Chie Takemoto, Shigeyuki Yokoyama
Journal of Bacteriology Aug 2007, 189 (17) 6397-6406; DOI: 10.1128/JB.00024-07

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Structural Characterization of the Ribosome Maturation Protein, RimM
Sakura Suzuki, Ayako Tatsuguchi, Eiko Matsumoto, Masahito Kawazoe, Tatsuya Kaminishi, Mikako Shirouzu, Yutaka Muto, Chie Takemoto, Shigeyuki Yokoyama
Journal of Bacteriology Aug 2007, 189 (17) 6397-6406; DOI: 10.1128/JB.00024-07
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KEYWORDS

Ribosomal Proteins
Thermus thermophilus

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