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Journal articles on the topic 'Gene expression in E. coli'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Al-Kanany, Fadhil N., and Rasha M. Othman. "Cloning and Expression of Pseudomonas aeruginosa AlkB Gene in E. coli." Journal of Pure and Applied Microbiology 14, no. 1 (2020): 389–96. http://dx.doi.org/10.22207/jpam.14.1.40.

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2

Kim, Kyung Hyuk, Kiri Choi, Bryan Bartley, and Herbert M. Sauro. "Controlling E. coli Gene Expression Noise." IEEE Transactions on Biomedical Circuits and Systems 9, no. 4 (2015): 497–504. http://dx.doi.org/10.1109/tbcas.2015.2461135.

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3

Ren, D., L. A. Bedzyk, S. M. Thomas, R. W. Ye, and T. K. Wood. "Gene expression in Escherichia coli biofilms." Applied Microbiology and Biotechnology 64, no. 4 (2004): 515–24. http://dx.doi.org/10.1007/s00253-003-1517-y.

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4

Schembri, Mark A., Kristian Kjaergaard, and Per Klemm. "Global gene expression in Escherichia coli biofilms." Molecular Microbiology 48, no. 1 (2003): 253–67. http://dx.doi.org/10.1046/j.1365-2958.2003.03432.x.

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5

Chen, K. S., P. Saxena, and J. R. Walker. "Expression of the Escherichia coli dnaX gene." Journal of Bacteriology 175, no. 20 (1993): 6663–70. http://dx.doi.org/10.1128/jb.175.20.6663-6670.1993.

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6

Løbner-Olesen, Anders, Erik Boye, and M. G. Marinus. "Expression of the Escherichia coli dam gene." Molecular Microbiology 6, no. 13 (1992): 1841–51. http://dx.doi.org/10.1111/j.1365-2958.1992.tb01356.x.

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7

Dewar, Susan J., and Robert Dorazi. "Control of division gene expression inEscherichia coli." FEMS Microbiology Letters 187, no. 1 (2000): 1–7. http://dx.doi.org/10.1111/j.1574-6968.2000.tb09127.x.

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8

EGOROV, A. M., I. G. GAZARYAN, S. V. SAVELYEV, V. A. FECHINA, A. N. VERYOVKIN, and B. B. KIM. "Horseradish Peroxidase Gene Expression in Escherichia coli." Annals of the New York Academy of Sciences 646, no. 1 Recombinant D (1991): 35–40. http://dx.doi.org/10.1111/j.1749-6632.1991.tb18561.x.

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9

LaVallie, Edward R., and John M. McCoy. "Gene fusion expression systems in Escherichia coli." Current Opinion in Biotechnology 6, no. 5 (1995): 501–6. http://dx.doi.org/10.1016/0958-1669(95)80083-2.

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10

Hao, Xiaoliang. "Influence of Some Point Mutations of Green Fluorescent Protein Gene on Expression Efficiency in Escherichia coli." International Journal of Chemical Engineering and Applications 7, no. 4 (2016): 259–63. http://dx.doi.org/10.18178/ijcea.2016.7.4.585.

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11

Roos, Viktoria, Charlotte I. J. Andersson, and Leif Bülow. "Gene expression profiling of Escherichia coli expressing double Vitreoscilla haemoglobin." Journal of Biotechnology 114, no. 1-2 (2004): 107–20. http://dx.doi.org/10.1016/j.jbiotec.2004.07.002.

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12

Ichinose, Masao, Kazumasa Miki, Yasuo Endo, et al. "Expression of cloned pepsinogen gene in Escherichia coli." SEIBUTSU BUTSURI KAGAKU 31, no. 6 (1987): 413–18. http://dx.doi.org/10.2198/sbk.31.413.

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13

Antonucci, T. K., P. Wen, and W. J. Rutter. "Eukaryotic promoters drive gene expression in Escherichia coli." Journal of Biological Chemistry 264, no. 30 (1989): 17656–59. http://dx.doi.org/10.1016/s0021-9258(19)84621-5.

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14

Johanningmeier, Udo. "Expression of the psbA Gene in E. coli." Zeitschrift für Naturforschung C 42, no. 7-8 (1987): 755–57. http://dx.doi.org/10.1515/znc-1987-7-801.

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A psbA gene fragment has been cloned into an expression vector in frame with the 3′end of the beta-galactosidase gene. Expression of this construct in E. coli results in an overproduction of a hybrid protein consisting of part of the herbicide binding protein and beta-galactosidase. An antiserum raised against this fusion protein specifically detects a 34 kDa polypeptide within the complex mixture of spinach thylakoid membrane proteins.

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15

Jørgensen, Flemming, and Charles G. Kurland. "Processivity errors of gene expression in Escherichia coli." Journal of Molecular Biology 215, no. 4 (1990): 511–21. http://dx.doi.org/10.1016/s0022-2836(05)80164-0.

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16

Chuang, S. E., D. L. Daniels, and F. R. Blattner. "Global regulation of gene expression in Escherichia coli." Journal of Bacteriology 175, no. 7 (1993): 2026–36. http://dx.doi.org/10.1128/jb.175.7.2026-2036.1993.

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17

Calmann, Melissa A., and M. G. Marinus. "Regulated Expression of the Escherichia coli dam Gene." Journal of Bacteriology 185, no. 16 (2003): 5012–14. http://dx.doi.org/10.1128/jb.185.16.5012-5014.2003.

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ABSTRACT Regulated expression of the Escherichia coli dam gene has been achieved with the araBAD promoter lacking a ribosome binding site. Cultures of dam mutants containing plasmid pMQ430 show no detectable methylation in the absence of arabinose and complete methylation in its presence. Dam methyltransferase is a substrate for the Lon protease.

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18

Gibert, I., M. Llagostera, and J. Barbé. "Regulation of ubiG gene expression in Escherichia coli." Journal of Bacteriology 170, no. 3 (1988): 1346–49. http://dx.doi.org/10.1128/jb.170.3.1346-1349.1988.

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19

Muraki, Michiro, Yoshifumi Jigami, Hideaki Tanaka, et al. "Expression of Synthetic Human Lysozyme Gene inEscherichia coli." Agricultural and Biological Chemistry 50, no. 3 (1986): 713–23. http://dx.doi.org/10.1080/00021369.1986.10867445.

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20

Vigal, T., J. F. Martin, and J. A. Gil. "Expression of theStreptomyces griseusÎ±-amylase gene inEscherichia coli." FEMS Microbiology Letters 118, no. 3 (1994): 259–63. http://dx.doi.org/10.1111/j.1574-6968.1994.tb06838.x.

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21

Schaffhausen, Brian, Thomas L. Benjamin, Jennifer Lodge, David Kaplan, and Thomas M. Roberts. "Expression of polyoma early gene products inE. coli." Nucleic Acids Research 13, no. 2 (1985): 501–19. http://dx.doi.org/10.1093/nar/13.2.501.

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22

Kondo, Tomo, and Shigehiko Yumura. "Strategies for enhancing gene expression in Escherichia coli." Applied Microbiology and Biotechnology 104, no. 9 (2020): 3825–34. http://dx.doi.org/10.1007/s00253-020-10430-4.

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23

Tabor, Jeffrey J., Anselm Levskaya, and Christopher A. Voigt. "Multichromatic Control of Gene Expression in Escherichia coli." Journal of Molecular Biology 405, no. 2 (2011): 315–24. http://dx.doi.org/10.1016/j.jmb.2010.10.038.

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24

Wong, Dominic W. S., Carl A. Batt, and John E. Kinsella. "Expression of the transglutaminase gene in Escherichia coli." International Journal of Biochemistry 23, no. 9 (1991): 947–53. http://dx.doi.org/10.1016/0020-711x(91)90084-z.

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25

Fumitaka, Kishimoto, Gomi Hideyuki, Kanaoka Masaharu, et al. "Direct expression of urogastrone gene in Escherichia coli." Gene 45, no. 3 (1986): 311–16. http://dx.doi.org/10.1016/0378-1119(86)90029-6.

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26

Nomura, Teruaki, Nobuyuki Fujita, and Akira Ishihama. "Expression of the leuX gene in Escherichia coli." Journal of Molecular Biology 197, no. 4 (1987): 659–70. http://dx.doi.org/10.1016/0022-2836(87)90472-4.

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27

Furuya, T., A. Hasegawa, M. Saitoh, et al. "Expression of feline immunodeficiency virusgag gene inEscherichia coli." Archives of Virology 122, no. 3-4 (1992): 383–90. http://dx.doi.org/10.1007/bf01317200.

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28

Johanningmeier, Udo. "Expression of the psbA Gene in E. coli." Zeitschrift für Naturforschung C 42, no. 6 (1987): 755–57. http://dx.doi.org/10.1515/znc-1987-0618.

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Abstract:

A psbA gene fragment has been cloned into an expression vector in frame with the 3′ end of the beta-galactosidase gene. Expression of this construct in E. coli results in an overproduction of a hybrid protein consisting of part of the herbicide binding protein and beta-galactosidase. An antiserum raised against this fusion protein specifically detects a 34 kDa polypeptide within the complex mixture of spinach thylakoid membrane proteins.

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29

Wellnitz, O., P. Reith, Haas SC, and Meyer HHD. "Immune relevant gene expression of mammary epithelial cells and their influence on leukocyte chemotaxis in response to different mastitis pathogens." Veterinární Medicína 51, No. 4 (2012): 125–32. http://dx.doi.org/10.17221/5531-vetmed.

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Different mastitis pathogens induce different courses of infection, i.e. more or less severe. Mammary epithelial cells play an important role in the initial combat against microorganisms by expression of cytokines and acute phase proteins that regulate the immune response. The objective of the present study was to investigate the involvement of the epithelial cells into the outcome of mastitis induced by different pathogens. Primary epithelial cell cultures isolated from milk were used to test the immune response by measuring the mRNA expression of immunomodulators and their influence on polym

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30

Dass, S. Balachandra, and R. Jayaraman. "Modulation of gene expression by the product offitA gene inEscherichia coli." Journal of Biosciences 12, no. 3 (1987): 229–37. http://dx.doi.org/10.1007/bf02703067.

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31

Cai, Jie, and Michael S. DuBow. "Expression of theEscherichia colichromosomalarsoperon." Canadian Journal of Microbiology 42, no. 7 (1996): 662–71. http://dx.doi.org/10.1139/m96-091.

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A chromosomally located operon (ars) of Escherichia coli has been previously shown to be functional in arsenic detoxification. DNA sequencing revealed three open reading frames homologous to the arsR, arsB, and arsC open reading frames of plasmid-based arsenic resistance operons isolated from both E. coli and staphylococcal species. To examine the outline of transcriptional regulation of the chromosomal ars operon, several transcriptional fusions, using the luciferase-encoding luxAB genes of Vibrio harveyi, were constructed. Measurement of the expression of these gene fusions demonstrated that

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32

Deriabin, O. M., O. G. Deryabina, and P. V. Gilchuk. "Cloning and expression of Erysipelothrix rhusiopathiae SPAA gene in Escherichia coli." Biopolymers and Cell 27, no. 4 (2011): 310–13. http://dx.doi.org/10.7124/bc.00010d.

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33

Choi, Young J., Lyne Morel, Teffanie Le FranÃ¯Â¿Â½ois, et al. "Novel, Versatile, and Tightly Regulated Expression System for Escherichia coli Strains." Applied and Environmental Microbiology 76, no. 15 (2010): 5058–66. http://dx.doi.org/10.1128/aem.00413-10.

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ABSTRACT A novel tightly regulated gene expression system was developed for Escherichia coli by applying the regulatory elements of the Pseudomonas putida F1 cym and cmt operons to control target gene expression at the transcriptional level by using p-isopropylbenzoate (cumate) as an inducer. This novel expression system, referred to as the cumate gene switch, includes a specific expression vector, pNEW, that contains a partial T5 phage promoter combined with the Pseudomonas-based synthetic operator and the cymR repressor protein-encoding gene designed to express constitutively in the host str

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34

Dusch, Nicole, Alfred Pühler та Jörn Kalinowski. "Expression of the Corynebacterium glutamicum panD Gene Encoding l-Aspartate-α-Decarboxylase Leads to Pantothenate Overproduction in Escherichia coli". Applied and Environmental Microbiology 65, № 4 (1999): 1530–39. http://dx.doi.org/10.1128/aem.65.4.1530-1539.1999.

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ABSTRACT The Corynebacterium glutamicum panD gene was identified by functional complementation of an Escherichia coli panDmutant strain. Sequence analysis revealed that the coding region ofpanD comprises 411 bp and specifies a protein of 136 amino acid residues with a deduced molecular mass of 14.1 kDa. A definedC. glutamicum panD mutant completely lackedl-aspartate-α-decarboxylase activity and exhibited β-alanine auxotrophy. The C. glutamicum panD(panDC.g. ) as well as the E. coli panD (panDE.c. ) genes were cloned into a bifunctional expression plasmid to allow gene analysis in C. glutamicum

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35

Liang, Lusha W., Razika Hussein, Dena H. S. Block, and Han N. Lim. "Minimal Effect of Gene Clustering on Expression inEscherichia coli." Genetics 193, no. 2 (2012): 453–65. http://dx.doi.org/10.1534/genetics.112.147199.

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36

Trung, Do Minh, Do Hai Quynh, Tran Viet Tien, Nguyen Duy Bac, Do Thi Tuyen, and Nguyen Thuy Duong. "Cloning and expression of pigC gene in Escherichia coli." Vietnam Journal of Biotechnology 16, no. 4 (2020): 757–65. http://dx.doi.org/10.15625/1811-4989/16/4/13488.

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Prodigiosin (Pg), which is particularly of interest because of anticancer and antimicrobial activities, can be produced through the PigC-catalyzed condensation reaction of 4-methoxy-2, 2’-bipyrrole-5-carboxyaldehyde (MBC) and 2-methyl-3-amylpyrrole (MAP). Therefore, the PigC protein plays an important role in prodigiosin biosynthetic pathway. However, studies related to PigC protein have not been carried out in Vietnam yet. In this work, the pigC gene was cloned and expressed in Escherichia coli DH10B and BL21 (DE3), respectively. Using PCR and universal primers, we amplified a fragment of 3 k

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37

Wȩgleńska, Anna, Biji Jacob, and Agnieszka Sirko. "Transcriptional pattern of Escherichia coli ihfB (himD) gene expression." Gene 181, no. 1-2 (1996): 85–88. http://dx.doi.org/10.1016/s0378-1119(96)00468-4.

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38

Kashiwagi, Akiko, Takahiro Sakurai, Saburo Tsuru, Bei-Wen Ying, Kotaro Mori, and Tetsuya Yomo. "Construction of Escherichia coli gene expression level perturbation collection." Metabolic Engineering 11, no. 1 (2009): 56–63. http://dx.doi.org/10.1016/j.ymben.2008.08.002.

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39

Lewin, Astrid, Thi Tuyen Tran, Daniela Jacob, Martin Mayer, Barbara Freytag, and Bernd Appel. "Yeast DNA sequences initiating gene expression in Escherichia coli." Microbiological Research 159, no. 1 (2004): 19–28. http://dx.doi.org/10.1016/j.micres.2004.01.006.

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40

MURAKI, Michiro, Yoshifumi JIGAMI, Hideaki TANAKA, et al. "Expression of synthetic human lysozyme gene in Escherichia coli." Agricultural and Biological Chemistry 50, no. 3 (1986): 713–23. http://dx.doi.org/10.1271/bbb1961.50.713.

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41

MURAKI, Michiro, Yoshifumi JIGAMI, Hideaki TANAKA, et al. "Expression of synthetic human lysozyme gene in Escherichia coli." Agricultural and Biological Chemistry 49, no. 9 (1985): 2829–31. http://dx.doi.org/10.1271/bbb1961.49.2829.

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42

Nieto, J. M., M. Carmona, S. Bolland, Y. Jubete, F. Cruz, and A. Juárez. "The hha gene modulates haemolysin expression in Escherichia coli." Molecular Microbiology 5, no. 5 (1991): 1285–93. http://dx.doi.org/10.1111/j.1365-2958.1991.tb01902.x.

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43

Yu, B. J., J. A. Kim, and J. G. Pan. "Signature gene expression profile of triclosan-resistant Escherichia coli." Journal of Antimicrobial Chemotherapy 65, no. 6 (2010): 1171–77. http://dx.doi.org/10.1093/jac/dkq114.

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44

Muraki, Michiro, Yoshifumi Jigami, Hideaki Tanaka, et al. "Expression of Synthetic Human Lysozyme Gene in Escherichia coli." Agricultural and Biological Chemistry 49, no. 9 (1985): 2829–31. http://dx.doi.org/10.1080/00021369.1985.10867176.

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45

Kudla, G., A. W. Murray, D. Tollervey, and J. B. Plotkin. "Coding-Sequence Determinants of Gene Expression in Escherichia coli." Science 324, no. 5924 (2009): 255–58. http://dx.doi.org/10.1126/science.1170160.

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46

Sano, T., and C. R. Cantor. "Expression of a cloned streptavidin gene in Escherichia coli." Proceedings of the National Academy of Sciences 87, no. 1 (1990): 142–46. http://dx.doi.org/10.1073/pnas.87.1.142.

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47

Domka, Joanna, Jintae Lee, Tarun Bansal, and Thomas K. Wood. "Temporal gene-expression in Escherichia coli K-12 biofilms." Environmental Microbiology 9, no. 2 (2007): 332–46. http://dx.doi.org/10.1111/j.1462-2920.2006.01143.x.

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48

Liao, X. Y., W. Shen, J. Chen, Y. Li, and G. C. Du. "Improved glutathione production by gene expression in Escherichia coli." Letters in Applied Microbiology 43, no. 2 (2006): 211–14. http://dx.doi.org/10.1111/j.1472-765x.2006.01927.x.

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49

Quinones, Ariel, Gudrun Wandt, Sabine Kleinstauber, and Walter Messer. "DnaA protein stimulates polA gene expression in Escherichia coli." Molecular Microbiology 23, no. 6 (1997): 1193–202. http://dx.doi.org/10.1046/j.1365-2958.1997.2961658.x.

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50

Pérez-Martinez, G., L. González-Candelas, J. Polaina, and A. Flors. "Expression of an endoglucanase gene fromClostridium cellulolyticum inEscherichia coli." Journal of Industrial Microbiology 3, no. 6 (1988): 365–71. http://dx.doi.org/10.1007/bf01569558.

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