227:
peptidyl-tRNA to puromycin. Furthermore, the chemical modification of half of these positions G2251, G2253, A2439, and U2584 can not prevent the tRNA binding. Peptidyl-tRNA of 50S subunits which binds to the P site preserve eight positions of 23S rRNA from chemical modification. On the other hand, mutation in 23S rRNA can also have impacts on cell growth. Mutations A1912G, A1919G and Ψ1917C have a powerful growth phenotypes and they prevent translation while mutation A1916G has a simple growth phenotype and it leads to defect in the 50S subunits.
69:
145:
25:
136:
235:
The 23S ribosomal RNA is composed of six domains forming a complex network of molecular interactions. A central single-stranded region connects all of the domains through base-pairing of the two halves, forming Helix 26a. Some consider Helix 26a to be Domain 0 due to its action as a central core and
226:
However, 23S rRNA positions (G2252, A2451, U2506, and U2585) have a significant function for tRNA binding in the P site of the large ribosomal subunit. These modification nucleotides in site P can inhibit peptidyl-tRNA from binding. U2555 modification can also intervene with transferring
217:
In general, rRNA has an essential function of peptidyl transferase. The stimulating core of the ribosome plays role in the peptide bond configuration. Both peptidyl-tRNA and aminoacyl-tRNA are important for protein synthesis and transpeptidation response.
190:, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Numerous mutations in domains of the 23S rRNA with Peptidyl transferase activity have resulted in
181:) of the bacterial/archean ribosome and makes up the peptidyl transferase center (PTC). The 23S rRNA is divided into six secondary structural domains titled I-VI, with the corresponding 5S rRNA being considered domain VII. The ribosomal
185:
activity resides in domain V of this rRNA, which is also the most common binding site for antibiotics that inhibit translation, making it a target for ribosomal engineering. A well-known member of this antibiotic class,
671:
Petrov, Anton S.; Bernier, Chad R.; Hershkovits, Eli; Xue, Yuzhen; Waterbury, Chris C.; Hsiao, Chiaolong; Stepanov, Victor G.; Gaucher, Eric A.; Grover, Martha A.; Harvey, Stephen C.; Hud, Nicholas V. (2013-06-14).
236:
compact folding unit. Comparison of 23S and 28S ribosomal RNA sequences across species demonstrate conservation of Helix 26a. Helices continue to provide the support as the backbone of domain architecture.
282:
Mueller F, Sommer I, Baranov P, Matadeen R, Stoldt M, Wöhnert J, Görlach M, van Heel M, Brimacombe R (2000). "The 3D arrangement of the 23 S and 5 S rRNA in the
819:
244:
Chloroplast ribosomes from "higher" plants have an additional 4.5S rRNA created by fragmentation of 23S. It is located to the 3' side of 23S in the
404:
501:
Doris, Stephen M.; Smith, Deborah R.; Beamesderfer, Julia N.; Raphael, Benjamin J.; Nathanson, Judith A.; Gerbi, Susan A. (October 2015).
153:
812:
194:. 23S rRNA genes typically have higher sequence variations, including insertions and/or deletions, compared to other rRNAs.
624:"Mutations in 23S rRNA at the Peptidyl Transferase Center and Their Relationship to Linezolid Binding and Cross-Resistance"
805:
391:
Zerges, William; Hauser, Charles (2009-01-01), Harris, Elizabeth H.; Stern, David B.; Witman, George B. (eds.),
191:
503:"Universal and domain-specific sequences in 23S–28S ribosomal RNA identified by computational phylogenetics"
1153:
1025:
39:
392:
1044:
148:
A 3D representation of the ribosome. This is a view of the 3D arrangement of the 23S and 5S rRNA in the
123:
568:
455:
337:
257:
182:
964:
991:
286:
50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 Å resolution".
206:
68:
1130:
1115:
1014:
996:
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731:"The complete structure of the chloroplast 70S ribosome in complex with translation factor pY"
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Long KS, Munck C, Andersen TM, Schaub MA, Hobbie SN, Bottger EC, Vester B (9 August 2010).
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Walker, Allison S.; Russ, William P.; Ranganathan, Rama; Schepartz, Alanna (2020-08-18).
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Please expand the article to include this information. Further details may exist on the
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Antibiotic
Resistance in Bacteria Caused by Modified Nucleosides in 23S Ribosomal RNA
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468:
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442:
Pei A, Nossa CW, Chokshi P, Blaser MJ, Yang L, Rosmarin DM, Pei Z (5 May 2009).
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561:
Proceedings of the
National Academy of Sciences of the United States of America
729:
Bieri, P; Leibundgut, M; Saurer, M; Boehringer, D; Ban, N (15 February 2017).
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168:
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590:
557:"23S rRNA positions essential for tRNA binding in ribosomal functional sites"
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23S and 5S rRNAs indicating nucleotide numbers, helix numbers, and domains
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Bocchetta, Maurizio; Xiong, Liqun; Mankin, Alexander S. (1998-03-31).
674:"Secondary structure and domain architecture of the 23S and 5S rRNAs"
673:
793:
Pseudobase entry for pseudoknot of the 23S ribosomal RNA (PKB00148)
444:"Diversity of 23S rRNA Genes within Individual Prokaryotic Genomes"
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about correct Rfam boxes: LSU_rRNA_archaea, LSU_rRNA_bacteria.
18:
16:
A component of the large subunit of the prokaryotic ribosome
248:
and corresponds to the 3' end of non-fragmented 23S rRNA.
326:"RNA sectors and allosteric function within the ribosome"
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393:"Chapter 28 - Protein Synthesis in the Chloroplast"
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330:Proceedings of the National Academy of Sciences
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399:, London: Academic Press, pp. 967–1025,
397:The Chlamydomonas Sourcebook (Second Edition)
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425:Vester, Birte; Long, Katherine S. (2013).
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154:cryo-electron microscopic reconstruction
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628:Antimicrobial Agents and Chemotherapy
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197:The eukaryotic homolog of the 23S
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152:50S ribosomal subunit based on a
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205:, with a region filled by the
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469:10.1371/journal.pone.0005437
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784:Page for 23S_ribosomal_RNA
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62:23S and 5S ribosomal RNAs
747:10.15252/embj.201695959
351:10.1073/pnas.1909634117
678:Nucleic Acids Research
582:10.1073/pnas.95.7.3525
520:10.1261/rna.051144.115
300:10.1006/jmbi.2000.3635
157:
34:is missing information
192:antibiotic resistance
147:
640:10.1128/AAC.00644-10
431:. Landes Bioscience.
258:23S methyl RNA motif
183:peptidyl transferase
1136:(See article table)
573:1998PNAS...95.3525B
460:2009PLoSO...4.5437P
342:2020PNAS..11719879W
336:(33): 19879–19887.
1131:Ribosomal proteins
690:10.1093/nar/gkt513
231:23S rRNA Helix 26a
213:23S rRNA Functions
207:5.8S ribosomal RNA
158:
1141:
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1125:
1124:
684:(15): 7522–7535.
634:(11): 4705–4713.
513:(10): 1719–1730.
406:978-0-12-370873-1
203:28S ribosomal RNA
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48:December 2020
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32:This article
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1059:MT-RNR1, 12S
1040:MT-RNR2, 16S
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1070:Chloroplast
965:Cytoplasmic
246:rRNA operon
167:is a 2,904
79:Identifiers
956:Eukaryotes
412:2021-10-07
288:J Mol Biol
269:References
169:nucleotide
133:structures
124:SO:0001263
84:Other data
698:1362-4962
591:0027-8424
360:0027-8424
171:long (in
107:Domain(s)
40:talk page
1148:Category
899:Bacteria
835:subunits
833:ribosome
765:28007896
716:23771137
658:20696869
539:26283689
488:19415112
448:PLOS ONE
378:32747536
308:10756104
263:LSU rRNA
252:See also
199:LSU rRNA
112:Bacteria
1054:(39S):
1045:MT-tRNA
1035:(28S):
842:Archaea
756:5694952
707:3753638
649:2976117
609:9520399
569:Bibcode
530:4574749
479:2672173
456:Bibcode
369:7443888
338:Bibcode
240:Plastid
201:is the
174:E. coli
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1105:Small
1077:Large
1072:(70S)
1052:Small
1033:Large
1028:(55S)
1004:Small
976:Large
934:Small
911:Large
877:Small
854:Large
600:19869
1093:4.5S
992:5.8S
982:):
788:Rfam
761:PMID
712:PMID
694:ISSN
654:PMID
605:PMID
587:ISSN
535:PMID
484:PMID
401:ISBN
374:PMID
356:ISSN
304:PMID
165:rRNA
160:The
137:PDBe
100:rRNA
96:Gene
92:type
1116:16S
1111:):
1109:30S
1098:23S
1083:):
1081:50S
1015:18S
1010:):
1008:40S
997:28S
980:60S
967:(80
945:16S
940:):
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917:):
915:50S
902:(70
888:16S
883:):
881:30S
870:23S
860:):
858:50S
845:(70
786:at
751:PMC
743:doi
702:PMC
686:doi
644:PMC
636:doi
595:PMC
577:doi
525:PMC
515:doi
507:RNA
474:PMC
464:doi
364:PMC
346:doi
334:117
296:doi
292:298
179:50S
162:23S
131:PDB
90:RNA
1150::
1088:5S
987:5S
922:5S
865:5S
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119:SO
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1107:(
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978:(
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