Ribosome

Most genes encoding ribosomal proteins are essential and many ribosomal proteins belong to the small set of universally conserved proteins.

Structure of the ribosome

• EMD-6306 (MifM-stalled ribosome complex) PubMed
• 3J9W (MifM-stalled ribosome complex) PubMed

Proteins of the large subunit

• L1
• L2
• L3
• L4
• L5
• L6
• L9
• L10
• L11
• L12
• L13
• L14
• L15
• L16
• L17
• L18
• L19
• L20
• L21
• L22
• L23
• L24
• L27
• L28
• L29
• L30
• L31
• L32
• L33a
• L33b
• L34
• L35
• L36

Proteins of the small subunit

• S2
• S3
• S4
• S5
• S6
• S7
• S8
• S9
• S10
• S11
• S12
• S13
• S14
• S15
• S16
• S17
• S18
• S19
• S20
• S21

Proteins that are part of the ribosome only under specific conditions

• Ctc: present in the large subunit under stress conditions
• RpmGC: replaces L33 under conditions of zinc limitation
• YbxF: L7 family, associated to the ribosome during logarithmic growth
• YhzA: replaces L31 under conditions of zinc limitation
• YtiA: replaces S14 under conditions of zinc limitation

Proteins that are similar to ribosomal proteins

• YfjL
• YlxQ
• YpfD

Related pages

• 5S rRNA
• 16S rRNA
• 23S rRNA
• translation

Important original publications

Daniel Sohmen, Shinobu Chiba, Naomi Shimokawa-Chiba, C Axel Innis, Otto Berninghausen, Roland Beckmann, Koreaki Ito, Daniel N Wilson
Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling.
Nat Commun: 2015, 6;6941
[PubMed:25903689] [WorldCat.org] [DOI] (I e)

Yury S Polikanov, Sergey V Melnikov, Dieter Söll, Thomas A Steitz
Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly.
Nat Struct Mol Biol: 2015, 22(4);342-344
[PubMed:25775268] [WorldCat.org] [DOI] (I p)

Jonas Noeske, Michael R Wasserman, Daniel S Terry, Roger B Altman, Scott C Blanchard, Jamie H D Cate
High-resolution structure of the Escherichia coli ribosome.
Nat Struct Mol Biol: 2015, 22(4);336-41
[PubMed:25775265] [WorldCat.org] [DOI] (I p)

Genki Akanuma, Ako Kobayashi, Shota Suzuki, Fujio Kawamura, Yuh Shiwa, Satoru Watanabe, Hirofumi Yoshikawa, Ryo Hanai, Morio Ishizuka
Defect in the formation of 70S ribosomes caused by lack of ribosomal protein L34 can be suppressed by magnesium.
J Bacteriol: 2014, 196(22);3820-30
[PubMed:25182490] [WorldCat.org] [DOI] (I p)

Yury S Polikanov, Thomas A Steitz, C Axel Innis
A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome.
Nat Struct Mol Biol: 2014, 21(9);787-93
[PubMed:25132179] [WorldCat.org] [DOI] (I p)

Kurt Fredrick, Michael Ibba
The ABCs of the ribosome.
Nat Struct Mol Biol: 2014, 21(2);115-6
[PubMed:24500425] [WorldCat.org] [DOI] (I p)

Lars V Bock, Christian Blau, Gunnar F Schröder, Iakov I Davydov, Niels Fischer, Holger Stark, Marina V Rodnina, Andrea C Vaiana, Helmut Grubmüller
Energy barriers and driving forces in tRNA translocation through the ribosome.
Nat Struct Mol Biol: 2013, 20(12);1390-6
[PubMed:24186064] [WorldCat.org] [DOI] (I p)

Ningning Li, Yuling Chen, Qiang Guo, Yixiao Zhang, Yi Yuan, Chengying Ma, Haiteng Deng, Jianlin Lei, Ning Gao
Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.
Nucleic Acids Res: 2013, 41(14);7073-83
[PubMed:23700310] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Koichi Yano, Shota Suzuki, Shuya Omata, Morio Ishizuka, Yasuhiko Sekine, Fujio Kawamura
Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation.
J Bacteriol: 2012, 194(22);6282-91
[PubMed:23002217] [WorldCat.org] [DOI] (I p)

Alex Rosenberg, Lior Sinai, Yoav Smith, Sigal Ben-Yehuda
Dynamic expression of the translational machinery during Bacillus subtilis life cycle at a single cell level.
PLoS One: 2012, 7(7);e41921
[PubMed:22848659] [WorldCat.org] [DOI] (I p)