Academic literature on the topic 'Anti-Shine Dalgarno'

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Journal articles on the topic "Anti-Shine Dalgarno"

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Weiner, Iddo, Noam Shahar, Pini Marco, Iftach Yacoby, and Tamir Tuller. "Solving the Riddle of the Evolution of Shine-Dalgarno Based Translation in Chloroplasts." Molecular Biology and Evolution 36, no. 12 (2019): 2854–60. http://dx.doi.org/10.1093/molbev/msz210.

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Abstract Chloroplasts originated from an ancient cyanobacterium and still harbor a bacterial-like genome. However, the centrality of Shine–Dalgarno ribosome binding, which predominantly regulates proteobacterial translation initiation, is significantly decreased in chloroplasts. As plastid ribosomal RNA anti-Shine–Dalgarno elements are similar to their bacterial counterparts, these sites alone cannot explain this decline. By computational simulation we show that upstream point mutations modulate the local structure of ribosomal RNA in chloroplasts, creating significantly tighter structures aro
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Stower, Hannah. "Anti-Shine–Dalgarno regulation of translation." Nature Reviews Genetics 13, no. 5 (2012): 298. http://dx.doi.org/10.1038/nrg3233.

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Praszkier, J., and A. J. Pittard. "Pseudoknot-Dependent Translational Coupling in repBA Genes of the IncB Plasmid pMU720 Involves Reinitiation." Journal of Bacteriology 184, no. 20 (2002): 5772–80. http://dx.doi.org/10.1128/jb.184.20.5772-5780.2002.

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ABSTRACT Replication of the IncB miniplasmid pMU720 requires synthesis of the replication initiator protein, RepA, whose translation is coupled to that of a leader peptide, RepB. The unusual feature of this system is that translational coupling in repBA has to be activated by the formation of a pseudoknot immediately upstream of the repA Shine-Dalgarno sequence. A small antisense RNA, RNAI, controls replication of pMU720 by interacting with repBA mRNA to inhibit expression of repA both directly, by preventing formation of the pseudoknot, and indirectly, by inhibiting translation of repB. The m
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Amin, Mohammad Ruhul, Alisa Yurovsky, Yuping Chen, Steve Skiena, and Bruce Futcher. "Re-annotation of 12,495 prokaryotic 16S rRNA 3’ ends and analysis of Shine-Dalgarno and anti-Shine-Dalgarno sequences." PLOS ONE 13, no. 8 (2018): e0202767. http://dx.doi.org/10.1371/journal.pone.0202767.

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Li, Gene-Wei, Eugene Oh, and Jonathan S. Weissman. "The anti-Shine–Dalgarno sequence drives translational pausing and codon choice in bacteria." Nature 484, no. 7395 (2012): 538–41. http://dx.doi.org/10.1038/nature10965.

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Petropoulos, Alexandros D., and Rachel Green. "Further in Vitro Exploration Fails to Support the Allosteric Three-site Model." Journal of Biological Chemistry 287, no. 15 (2012): 11642–48. http://dx.doi.org/10.1074/jbc.c111.330068.

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Ongoing debate in the ribosome field has focused on the role of bound E-site tRNA and the Shine-Dalgarno-anti-Shine-Dalgarno (SD-aSD) interaction on A-site tRNA interactions and the fidelity of tRNA selection. Here we use an in vitro reconstituted Escherichia coli translation system to explore the reported effects of E-site-bound tRNA and SD-aSD interactions on tRNA selection events and find no evidence for allosteric coupling. A large set of experiments exploring the role of the E-site tRNA in miscoding failed to recapitulate the observations of earlier studies (Di Giacco, V., Márquez, V., Qi
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Moll, Isabella, Michael Huber, Sonja Grill, et al. "Evidence against an Interaction between the mRNA Downstream Box and 16S rRNA in Translation Initiation." Journal of Bacteriology 183, no. 11 (2001): 3499–505. http://dx.doi.org/10.1128/jb.183.11.3499-3505.2001.

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ABSTRACT Based on the complementarity of the initial coding region (downstream box [db]) of several bacterial and phage mRNAs to bases 1469 to 1483 in helix 44 of 16S rRNA (anti-downstream box [adb]), it has been proposed that db-adb base pairing enhances translation in a way that is similar to that of the Shine-Dalgarno (SD)/anti-Shine-Dalgarno (aSD) interaction. Computer modeling of helix 44 on the 30S subunit shows that the topography of the 30S ribosome does not allow a simultaneous db-adb interaction and placement of the initiation codon in the ribosomal P site. Thus, the db-adb interacti
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Poot, Raymond A., Marcel F. Brink, Cornelis W. A. Pleji, Herman A. de Boer, and Jan Van Duin. "Separation of mutant and wild-type ribosomes based on differences in their anti Shine - Dalgarno sequence." Nucleic Acids Research 21, no. 23 (1993): 5398–402. http://dx.doi.org/10.1093/nar/21.23.5398.

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Stefan, Alessandra, Flavio Schwarz, Daniela Bressanin, and Alejandro Hochkoeppler. "Shine-Dalgarno sequence enhances the efficiency of lacZ repression by artificial anti-lac antisense RNAs in Escherichia coli." Journal of Bioscience and Bioengineering 110, no. 5 (2010): 523–28. http://dx.doi.org/10.1016/j.jbiosc.2010.05.012.

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Skorski, Patricia, Prune Leroy, Olivier Fayet, Marc Dreyfus, and Sylvie Hermann-Le Denmat. "The Highly Efficient Translation Initiation Region from the Escherichia coli rpsA Gene Lacks a Shine-Dalgarno Element." Journal of Bacteriology 188, no. 17 (2006): 6277–85. http://dx.doi.org/10.1128/jb.00591-06.

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ABSTRACT The translational initiation region (TIR) of the Escherichia coli rpsA gene, which encodes ribosomal protein S1, shows a number of unusual features. It extends far upstream (to position −91) of the initiator AUG, it lacks a canonical Shine-Dalgarno sequence (SD) element, and it can fold into three successive hairpins (I, II, and III) that are essential for high translational activity. Two conserved GGA trinucleotides, present in the loops of hairpins I and II, have been proposed to form a discontinuous SD. Here, we have tested this hypothesis with the “specialized ribosome” approach.
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Dissertations / Theses on the topic "Anti-Shine Dalgarno"

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Abolbaghaei, Akram. "Shine-Dalgarno Anti-Shine-Dalgarno Sequence Interactions and Their Functional Role in Translational Efficiency of Bacteria and Archaea." Thesis, Université d'Ottawa / University of Ottawa, 2016. http://hdl.handle.net/10393/35254.

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Translation is a crucial factor in determining the rate of protein biosynthesis; for this reason, bacterial species typically evolve features to improve translation efficiency. Biosynthesis is a finely tuned cellular process aimed at providing the cell with an appropriate amount of proteins and RNAs to fulfill all of its metabolic functions. A key bacterial feature for faster recognition of the start codon on mRNA is the binding between the anti-Shine-Dalgarno (aSD) sequence on prokaryotic ribosomes at the 3’ end of the small subunit (SSU) 16S rRNA and Shine-Dalgarno (SD) sequence, a purine-ri
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Shah, Riyaz Ahmad. "Role of conserved features of initiator tRNA and ribosome heterogeneity in translation initiation in Escherichia coli." Thesis, 2018. https://etd.iisc.ac.in/handle/2005/5290.

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Translation is one of the fundamental and core cellular processes catalysed by a ribonucleoprotein complex called ribosome. The process involves four major steps: initiation, elongation, termination and recycling. Initiation is the rate limiting step in translation, which determines the correct reading frame in an mRNA. Initiation occurs by formation of an initiation complex comprising 30S ribosomal subunit, mRNA, initiator tRNA, and initiation factors. The recruitment of 30S ribosomal subunit to the mRNA is aided by interaction between conserved RNA sequence called anti-Shine Dalgarno (aSD) i
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Book chapters on the topic "Anti-Shine Dalgarno"

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"Anti-Shine–Dalgarno Sequence." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_976.

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