Relevant bibliographies by topics / Tryptophan operon repressor (TrpR)

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Academic literature on the topic 'Tryptophan operon repressor (TrpR)'

Author: Grafiati
Published: 4 June 2025
Last updated: 1 August 2025

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Journal articles on the topic "Tryptophan operon repressor (TrpR)"

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Akers, Johnny C., and Ming Tan. "Molecular Mechanism of Tryptophan-Dependent Transcriptional Regulation in Chlamydia trachomatis." Journal of Bacteriology 188, no. 12 (2006): 4236–43. http://dx.doi.org/10.1128/jb.01660-05.

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ABSTRACT Tryptophan is an essential amino acid that is required for normal development in Chlamydia species, and tryptophan metabolism has been implicated in chlamydial persistence and tissue tropism. The ability to synthesize tryptophan is not universal among the Chlamydiaceae, but species that have a predicted tryptophan biosynthetic pathway also encode an ortholog of TrpR, a regulator of tryptophan metabolism in many gram-negative bacteria. We show that in Chlamydia trachomatis serovar D, TrpR regulates its own gene and trpB and trpA, the genes for the two subunits of tryptophan synthase. T
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Sherchand, Shardulendra P., and Ashok Aiyar. "Ammonia generation by tryptophan synthase drives a key genetic difference between genital and ocular Chlamydia trachomatis isolates." Proceedings of the National Academy of Sciences 116, no. 25 (2019): 12468–77. http://dx.doi.org/10.1073/pnas.1821652116.

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A striking difference between genital and ocular clinical isolates of Chlamydia trachomatis is that only the former express a functional tryptophan synthase and therefore can synthesize tryptophan by indole salvage. Ocular isolates uniformly cannot use indole due to inactivating mutations within tryptophan synthase, indicating a selection against maintaining this enzyme in the ocular environment. Here, we demonstrate that this selection occurs in two steps. First, specific indole derivatives, produced by the human gut microbiome and present in serum, rapidly induce expression of C. trachomatis
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Brune, Iris, Nina Jochmann, Karina Brinkrolf, et al. "The IclR-Type Transcriptional Repressor LtbR Regulates the Expression of Leucine and Tryptophan Biosynthesis Genes in the Amino Acid Producer Corynebacterium glutamicum." Journal of Bacteriology 189, no. 7 (2007): 2720–33. http://dx.doi.org/10.1128/jb.01876-06.

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ABSTRACT The transcriptional regulator Cg1486 of Corynebacterium glutamicum ATCC 13032 is a member of the IclR protein family and belongs to the conserved set of regulatory proteins in corynebacteria. A defined deletion in the cg1486 gene, now designated ltbR (leucine and tryptophan biosynthesis regulator), led to the mutant strain C. glutamicum IB1486. According to whole-genome expression analysis by DNA microarray hybridizations, transcription of the leuB and leuCD genes encoding enzymes of the leucine biosynthesis pathway was enhanced in C. glutamicum IB1486 compared with the wild-type stra
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Xie, Yunwei, and John N. Reeve. "Regulation of Tryptophan Operon Expression in the Archaeon Methanothermobacter thermautotrophicus." Journal of Bacteriology 187, no. 18 (2005): 6419–29. http://dx.doi.org/10.1128/jb.187.18.6419-6429.2005.

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ABSTRACT Conserved trp genes encode enzymes that catalyze tryptophan biosynthesis in all three biological domains, and studies of their expression in Bacteria and eukaryotes have revealed a variety of different regulatory mechanisms. The results reported here provide the first detailed description of an archaeal trp gene regulatory system. We have established that the trpEGCFBAD operon in Methanothermobacter thermautotrophicus is transcribed divergently from a gene (designated trpY) that encodes a tryptophan-sensitive transcription regulator. TrpY binds to TRP box sequences (consensus, TGTACA)
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Sprenger, Janina, Catherine L. Lawson, Claes von Wachenfeldt, Leila Lo Leggio, and Jannette Carey. "Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan." Acta Crystallographica Section F Structural Biology Communications 77, no. 7 (2021): 215–25. http://dx.doi.org/10.1107/s2053230x21006142.

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The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand L-tryptophan (L-Trp) indicate that L-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts. This result is unexpected because the ligand binding-site residues arise from three separate polypeptide chains in the domain-swapped form. This work represents the first published structure of a domain-swapped form of TrpR with L-Trp bound. The presented structures also show that the protein amino
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Su, Panpan, Zhiwei Song, Guichun Wu, et al. "Insights Into the Roles of Two Genes of the Histidine Biosynthesis Operon in Pathogenicity of Xanthomonas oryzae pv. oryzicola." Phytopathology® 108, no. 5 (2018): 542–51. http://dx.doi.org/10.1094/phyto-09-17-0332-r.

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Xanthomonas oryzae pv. oryzicola is an X. oryzae pathovar that causes bacterial leaf streak in rice. In this study, we performed functional characterization of a nine-gene his operon in X. oryzae pv. oryzicola. Sequence analysis indicates that this operon is highly conserved in Xanthomonas spp. Auxotrophic assays confirmed that the his operon was involved in histidine biosynthesis. We found that two genes within this operon, trpR and hisB, were required for virulence and bacterial growth in planta. Further research revealed that trpR and hisB play different roles in X. oryzae pv. oryzicola. Th
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Arvidson, D. N., M. Shapiro, and P. Youderian. "Mutant tryptophan aporepressors with altered specificities of corepressor recognition." Genetics 128, no. 1 (1991): 29–35. http://dx.doi.org/10.1093/genetics/128.1.29.

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Abstract The Escherichia coli trpR gene encodes tryptophan aporepressor, which binds the corepressor ligand, L-tryptophan, to form an active repressor complex. The side chain of residue valine 58 of Trp aporepressor sits at the bottom of the corepressor (L-tryptophan) binding pocket. Mutant trpR genes encoding changes of Val58 to the other 19 naturally occurring amino acids were made. Each of the mutant proteins requires a higher intracellular concentration of tryptophan for activation of DNA binding than wild-type aporepressor. Whereas wild-type aporepressor is activated better by 5-methyltry
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Tripet, Brian P., Anupam Goel, and Valérie Copié. "Internal Dynamics of the Tryptophan Repressor (TrpR) and Two Functionally Distinct TrpR Variants, L75F-TrpR and A77V-TrpR, in Theirl-Trp-Bound Forms." Biochemistry 50, no. 23 (2011): 5140–53. http://dx.doi.org/10.1021/bi200389k.

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Copie, Valerie, Brian Tripet, Anupam Goel, Lucas Nerbert, and Jannette Carey. "Dynamical Studies Of A Temperature-Sensitive Mutant Of The Tryptophan Repressor Protein, L75F-TrpR." Biophysical Journal 96, no. 3 (2009): 322a. http://dx.doi.org/10.1016/j.bpj.2008.12.1618.

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Grove, C. L., and R. P. Gunsalus. "Regulation of the aroH operon of Escherichia coli by the tryptophan repressor." Journal of Bacteriology 169, no. 5 (1987): 2158–64. http://dx.doi.org/10.1128/jb.169.5.2158-2164.1987.

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Book chapters on the topic "Tryptophan operon repressor (TrpR)"

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Gryk, M. R., and O. Jardetzky. "Flexibility and Function of the Excherichia coli trp Represser." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0011.

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The trp repressor from Escherichia coli is a DNA binding protein, which in the presence of the ami no acid tryptophan inhibits the transcription of at least five operons: trpEDCBA, trpR, aroH, mtr, and aroL (Zubay et al., 1972; Rose et al., 1973; Zurawski et al., 1981; Heatwole and Somerville, 1991, 1992). The ligand-free form (aporepressor) shows only weak binding (KD ~ 106 - 107 M) to DNA, independent of the nucleotide sequence (Carey, 1988; Hurlburt and Yanofsky, 1990). The tryptophan containing form (holorepressor) binds preferentially to specific operator sequences with a much higher bind
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Revington, M. J., and W. Lee. "Heteronuclear Strategies for the Assignment of Larger protein/DNA complexes: Application to the 37 kDa trp Represser-Operator Complex." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0012.

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The sequence-specific DNA binding function of many proteins is recognized as one of the central mechanisms of regulating transcription and DNA replication and repair. The ability of these proteins to select a short (usually 10 to 20 basepair) sequence out of the entire genome with which to form a stable complex is a prime example of molecular recognition. Atomic resolution structural studies using NMR and X-ray crystallography have emerged as essential techniques in understanding the basis of specificity and stability in these systems. While NMR studies of small DNA-binding domains of proteins
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Conference papers on the topic "Tryptophan operon repressor (TrpR)"

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Pannekok, H., A. J. Van Zonneveid, C. J. M. de vries, M. E. MacDonald, H. Veerman, and F. Blasi. "FUNCTIONAL PROPERTIES OF DELETION-MUTANTS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643724.

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Over the past twenty-five years, genetic methods have generated a wealth of information on the regulation and the structure-function relationship of bacterial genes.These methods are based on the introduction of random mutations in a gene to alter its function. Subsequently, genetic techniques cure applied to localize the mutation, while the nature of the impairedfunction could be determined using biochemical methods. Classic examples of this approach is now considered to be the elucidation of the structure and function of genes, constituting the Escherichia coli lactose (lac) and tryptophan (
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