Difference between revisions of "Ribosome"
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− | <pubmed>22848659 23420519 23002217 23700310 </pubmed> | + | <pubmed>22848659 23420519 23002217 23700310 24186064 </pubmed> |
==Reviews on ribosome structure and function== | ==Reviews on ribosome structure and function== | ||
<pubmed> 19838167 17574829 16962654 16959973 12370012 20393556 19653700 21529161 21548786 23433801 23700310 </pubmed> | <pubmed> 19838167 17574829 16962654 16959973 12370012 20393556 19653700 21529161 21548786 23433801 23700310 </pubmed> |
Revision as of 13:50, 8 January 2014
Most genes encoding ribosomal proteins are essential and many ribosomal proteins belong to the small set of universally conserved proteins.
Contents
- 1 Structure of the ribosome
- 2 Proteins of the large subunit
- 3 Proteins of the small subunit
- 4 Proteins that are part of the ribosome only under specific conditions
- 5 Proteins that are similar to ribosomal proteins
- 6 Related pages
- 7 Back to Protein-protein interactions
- 8 Important original publications
- 9 Reviews on ribosome structure and function
Structure of the ribosome
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
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
Related pages
Back to Protein-protein interactions
Important original publications
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)
Reviews on ribosome structure and function