Ribosome

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

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

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)

Reviews on ribosome structure and function

Katelyn McGary, Evgeny Nudler
RNA polymerase and the ribosome: the close relationship.
Curr Opin Microbiol: 2013, 16(2);112-7
[PubMed:23433801] [WorldCat.org] [DOI] (I p)

Edward Ki Yun Leung, Nikolai Suslov, Nicole Tuttle, Raghuvir Sengupta, Joseph Anthony Piccirilli
The mechanism of peptidyl transfer catalysis by the ribosome.
Annu Rev Biochem: 2011, 80;527-55
[PubMed:21548786] [WorldCat.org] [DOI] (I p)

Zahra Shajani, Michael T Sykes, James R Williamson
Assembly of bacterial ribosomes.
Annu Rev Biochem: 2011, 80;501-26
[PubMed:21529161] [WorldCat.org] [DOI] (I p)

Sotaro Uemura, Colin Echeverría Aitken, Jonas Korlach, Benjamin A Flusberg, Stephen W Turner, Joseph D Puglisi
Real-time tRNA transit on single translating ribosomes at codon resolution.
Nature: 2010, 464(7291);1012-7
[PubMed:20393556] [WorldCat.org] [DOI] (I p)

T Martin Schmeing, V Ramakrishnan
What recent ribosome structures have revealed about the mechanism of translation.
Nature: 2009, 461(7268);1234-42
[PubMed:19838167] [WorldCat.org] [DOI] (I p)

Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700] [WorldCat.org] [DOI] (P p)

Veysel Berk, Jamie H D Cate
Insights into protein biosynthesis from structures of bacterial ribosomes.
Curr Opin Struct Biol: 2007, 17(3);302-9
[PubMed:17574829] [WorldCat.org] [DOI] (P p)

Andrei Korostelev, Sergei Trakhanov, Martin Laurberg, Harry F Noller
Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements.
Cell: 2006, 126(6);1065-77
[PubMed:16962654] [WorldCat.org] [DOI] (P p)

Maria Selmer, Christine M Dunham, Frank V Murphy, Albert Weixlbaumer, Sabine Petry, Ann C Kelley, John R Weir, V Ramakrishnan
Structure of the 70S ribosome complexed with mRNA and tRNA.
Science: 2006, 313(5795);1935-42
[PubMed:16959973] [WorldCat.org] [DOI] (I p)

Ada Yonath
High-resolution structures of large ribosomal subunits from mesophilic eubacteria and halophilic archaea at various functional States.
Curr Protein Pept Sci: 2002, 3(1);67-78
[PubMed:12370012] [WorldCat.org] [DOI] (P p)