Structural insight into the role of the ribosomal tunnel in cellular regulation (704 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
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Paper type: Journal Article,
Impact factor: 11.579, 5-year impact factor: 13
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037407668&partnerID=40&md5=a06b97073a8686a4af5da9ba75c33f39
Keywords: Antibiotic Agent, Azithromycin, Erythromycin, Macrolide, Ribosome Protein, Ribosome Rna, Troleandomycin, Article, Biosynthesis, Cell, Crystal Structure, Deinococcus Radiodurans, Drug Binding, Drug Protein Binding, Nonhuman, Priority Journal, Protein Structure, Regulatory Mechanism, Structure Analysis, Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Ribosomal Proteins, Signal Transduction,
Affiliations:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
Institute of Biochemistry, Free University, Berlin, Germany
References:
Not available.
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 11.579, 5-year impact factor: 13
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0037407668&partnerID=40&md5=a06b97073a8686a4af5da9ba75c33f39
Keywords: Antibiotic Agent, Azithromycin, Erythromycin, Macrolide, Ribosome Protein, Ribosome Rna, Troleandomycin, Article, Biosynthesis, Cell, Crystal Structure, Deinococcus Radiodurans, Drug Binding, Drug Protein Binding, Nonhuman, Priority Journal, Protein Structure, Regulatory Mechanism, Structure Analysis, Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Ribosomal Proteins, Signal Transduction,
Affiliations:
*** IBB - CNR ***
Max-Planck-Res. U. Ribosomal Struct., Hamburg, Germany
Inst. of Biostructure and Bioimaging, CNR, Napoli, Italy
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel
Institute of Biochemistry, Free University, Berlin, Germany
References:
Not available.
Structural insight into the role of the ribosomal tunnel in cellular regulation
Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallographically. The results provide insights into the tunnel dynamics at high resolution. Here we show that, in addition to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved β-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism.
Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallographically. The results provide insights into the tunnel dynamics at high resolution. Here we show that, in addition to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved β-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism.
Structural insight into the role of the ribosomal tunnel in cellular regulation
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Structural insight into the role of the ribosomal tunnel in cellular regulation
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Agmon I, Amit M, Auerbach T, Bashan A, Baram D, Bartels H, Berisio R, Greenberg I, Harms J, Hansen HAS, Kessler M, Pyetan E, Schluenzen F, Sittner A, Yonath A, Zarivach R
* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (636 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (847 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen HAS, Fucini P, Yonath A
* Structural insight into the antibiotic action of telithromycin against resistant mutants (849 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
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Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
* Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (738 views)
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
Impact Factor: 16.835
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Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (749 views)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
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32 Records (30 excluding Abstracts).
Total impact factor: 116.419 (110.292 excluding Abstracts).
Total 5 year impact factor: 121.53 (115.184 excluding Abstracts).
Total impact factor: 116.419 (110.292 excluding Abstracts).
Total 5 year impact factor: 121.53 (115.184 excluding Abstracts).
704 views. Last view on Tuesday 22 April 2025, 0:06:19
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