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Journal articles on the topic 'Proteins Escherichia coli'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 January 2023

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1

Siegele, Deborah A. "Universal Stress Proteins in Escherichia coli." Journal of Bacteriology 187, no. 18 (2005): 6253–54. http://dx.doi.org/10.1128/jb.187.18.6253-6254.2005.

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2

Blair, D. F., D. Y. Kim, and H. C. Berg. "Mutant MotB proteins in Escherichia coli." Journal of Bacteriology 173, no. 13 (1991): 4049–55. http://dx.doi.org/10.1128/jb.173.13.4049-4055.1991.

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3

Tang, Fengyi, and Milton H. Saier. "Transport proteins promoting Escherichia coli pathogenesis." Microbial Pathogenesis 71-72 (June 2014): 41–55. http://dx.doi.org/10.1016/j.micpath.2014.03.008.

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4

Gill, Stanley C., Stephen E. Weitzel та Peter H. von Hippel. "Escherichia coli σ70 and NusA proteins". Journal of Molecular Biology 220, № 2 (1991): 307–24. http://dx.doi.org/10.1016/0022-2836(91)90015-x.

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5

Gill, Stanley C., Thomas D. Yager та Peter H. von Hippel. "Escherichia coli σ70 and NusA proteins". Journal of Molecular Biology 220, № 2 (1991): 325–33. http://dx.doi.org/10.1016/0022-2836(91)90016-y.

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6

Hayat, Seyed Mohammad Gheibi, Najmeh Farahani, Behrouz Golichenari, and Amirhossein Sahebkar. "Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know." Current Pharmaceutical Design 24, no. 6 (2018): 718–25. http://dx.doi.org/10.2174/1381612824666180131121940.

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Background: Host, vector, and culture conditions (including cultivation media) are considered among the three main elements contributing to a successful production of recombinant proteins. Accordingly, one of the most common hosts to produce recombinant therapeutic proteins is Escherichia coli. Methodology: A comprehensive literature review was performed to identify important factors affecting production of recombinant proteins in Escherichia coli. Results: Escherichia coli is taken into account as the easiest, quickest, and cheapest host with a fully known genome. Thus, numerous modifications

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7

Schumann, Wolfgang, and Luis Carlos S. Ferreira. "Production of recombinant proteins in Escherichia coli." Genetics and Molecular Biology 27, no. 3 (2004): 442–53. http://dx.doi.org/10.1590/s1415-47572004000300022.

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8

BANEYX, FRANÇOIS, and GEORGE GEORGIOU. "Degradation of Secreted Proteins in Escherichia coli." Annals of the New York Academy of Sciences 665, no. 1 Biochemical E (1992): 301–8. http://dx.doi.org/10.1111/j.1749-6632.1992.tb42593.x.

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9

Weber, Richard F., and Philip M. Silverman. "The Cpx proteins of Escherichia coli K12." Journal of Molecular Biology 203, no. 2 (1988): 467–78. http://dx.doi.org/10.1016/0022-2836(88)90013-7.

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10

Riley, M. "Genes and proteins of Escherichia coli (GenProtEc)." Nucleic Acids Research 24, no. 1 (1996): 40. http://dx.doi.org/10.1093/nar/24.1.40.

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11

PAGES, Jean Marie, and Claude LAZDUNSKI. "Maturation of Exported Proteins in Escherichia coli." European Journal of Biochemistry 124, no. 3 (2005): 561–66. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06630.x.

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12

Stamford, N. Patrick J., J. Stamford, Penelope E. Lilley, and Nicholas E. Dixon. "Enriched sources of Escherichia coli replication proteins." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1132, no. 1 (1992): 17–25. http://dx.doi.org/10.1016/0167-4781(92)90047-4.

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13

Awano, Naoki, Vaishnavi Rajagopal, Mark Arbing, et al. "Escherichia coli RNase R Has Dual Activities, Helicase and RNase." Journal of Bacteriology 192, no. 5 (2009): 1344–52. http://dx.doi.org/10.1128/jb.01368-09.

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ABSTRACT In Escherichia coli, the cold shock response occurs when there is a temperature downshift from 37°C to 15°C, and this response is characterized by induction of several cold shock proteins, including the DEAD-box helicase CsdA, during the acclimation phase. CsdA is involved in a variety of cellular processes. Our previous studies showed that the helicase activity of CsdA is critical for its function in cold shock acclimation of cells and that the only proteins that were able to complement its function were another helicase, RhlE, an RNA chaperone, CspA, and a cold-inducible exoribonucl

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14

Park, Jin-Seung, Kyung-Yeon Han, Jong-Am Song, Keum-Young Ahn, Hyuk-Seong Seo, and Jeewon Lee. "Escherichia coli malate dehydrogenase, a novel solubility enhancer for heterologous proteins synthesized in Escherichia coli." Biotechnology Letters 29, no. 10 (2007): 1513–18. http://dx.doi.org/10.1007/s10529-007-9417-3.

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15

Kamionka, Mariusz. "Engineering of Therapeutic Proteins Production in Escherichia coli." Current Pharmaceutical Biotechnology 12, no. 2 (2011): 268–74. http://dx.doi.org/10.2174/138920111794295693.

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16

Yoon, Sung, Seong Kim, and Jihyun Kim. "Secretory Production of Recombinant Proteins in Escherichia coli." Recent Patents on Biotechnology 4, no. 1 (2010): 23–29. http://dx.doi.org/10.2174/187220810790069550.

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17

Carré, Gaëlle, Erwann Hamon, Saïd Ennahar, et al. "TiO2Photocatalysis Damages Lipids and Proteins in Escherichia coli." Applied and Environmental Microbiology 80, no. 8 (2014): 2573–81. http://dx.doi.org/10.1128/aem.03995-13.

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ABSTRACTThis study investigates the mechanisms of UV-A (315 to 400 nm) photocatalysis with titanium dioxide (TiO2) applied to the degradation ofEscherichia coliand their effects on two key cellular components: lipids and proteins. The impact of TiO2photocatalysis onE. colisurvival was monitored by counting on agar plate and by assessing lipid peroxidation and performing proteomic analysis. We observed through malondialdehyde quantification that lipid peroxidation occurred during the photocatalytic process, and the addition of superoxide dismutase, which acts as a scavenger of the superoxide an

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18

de Gier, Jan-Willem, and Joen Luirink. "Biogenesis of inner membrane proteins in Escherichia coli." Molecular Microbiology 40, no. 2 (2001): 314–22. http://dx.doi.org/10.1046/j.1365-2958.2001.02392.x.

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19

Nesterchuk, M. V., P. V. Sergiev, and O. A. Dontsova. "Posttranslational Modifications of Ribosomal Proteins in Escherichia coli." Acta Naturae 3, no. 2 (2011): 22–33. http://dx.doi.org/10.32607/20758251-2011-3-2-22-33.

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20

Hengge-Aronis, R., and W. Boos. "Translational control of exported proteins in Escherichia coli." Journal of Bacteriology 167, no. 2 (1986): 462–66. http://dx.doi.org/10.1128/jb.167.2.462-466.1986.

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21

Swartz, James R. "Advances in Escherichia coli production of therapeutic proteins." Current Opinion in Biotechnology 12, no. 2 (2001): 195–201. http://dx.doi.org/10.1016/s0958-1669(00)00199-3.

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22

Georgiou, George, and Pascal Valax. "Expression of correctly folded proteins in Escherichia coli." Current Opinion in Biotechnology 7, no. 2 (1996): 190–97. http://dx.doi.org/10.1016/s0958-1669(96)80012-7.

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23

Berkmen, Mehmet. "Production of disulfide-bonded proteins in Escherichia coli." Protein Expression and Purification 82, no. 1 (2012): 240–51. http://dx.doi.org/10.1016/j.pep.2011.10.009.

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24

Tarry, Michael, Karin Skaar, Gunnar von Heijne, Roger R. Draheim, and Martin Högbom. "Production of human tetraspanin proteins in Escherichia coli." Protein Expression and Purification 82, no. 2 (2012): 373–79. http://dx.doi.org/10.1016/j.pep.2012.02.003.

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25

Adams, Hendrik, Wieke Teertstra, Jeroen Demmers, Rolf Boesten, and Jan Tommassen. "Interactions between Phage-Shock Proteins in Escherichia coli." Journal of Bacteriology 185, no. 4 (2003): 1174–80. http://dx.doi.org/10.1128/jb.185.4.1174-1180.2003.

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ABSTRACT Expression of the pspABCDE operon of Escherichia coli is induced upon infection by filamentous phage and by many other stress conditions, including defects in protein export. Expression of the operon requires the alternative sigma factor σ54 and the transcriptional activator PspF. In addition, PspA plays a negative regulatory role, and the integral-membrane proteins PspB and PspC play a positive one. In this study, we investigated whether the suggested protein-protein interactions implicated in this complex regulatory network can indeed be demonstrated. Antisera were raised against Ps

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26

Spector, Shari, Julia M. Flynn, Bruce Tidor, Tania A. Baker, and Robert T. Sauer. "Expression of N-formylated proteins in Escherichia coli." Protein Expression and Purification 32, no. 2 (2003): 317–22. http://dx.doi.org/10.1016/j.pep.2003.08.004.

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27

Harmon, Alice C., Douglas Prasher, and Milton J. Cormier. "High-affinity calcium-binding proteins in escherichia coli." Biochemical and Biophysical Research Communications 127, no. 1 (1985): 31–36. http://dx.doi.org/10.1016/s0006-291x(85)80121-2.

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28

Scott Champney, W. "Reversed-phase chromatography of Escherichia coli ribosomal proteins." Journal of Chromatography A 522 (November 1990): 163–70. http://dx.doi.org/10.1016/0021-9673(90)85186-y.

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29

Davies, K. "Degradation of oxidatively denatured proteins in Escherichia coli." Free Radical Biology and Medicine 5, no. 4 (1988): 215–23. http://dx.doi.org/10.1016/0891-5849(88)90015-9.

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30

Rosenwasser, T. A., K. A. Hogquist, S. F. Nothwehr, et al. "Compartmentalization of mammalian proteins produced in Escherichia coli." Journal of Biological Chemistry 265, no. 22 (1990): 13066–73. http://dx.doi.org/10.1016/s0021-9258(19)38268-7.

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31

Galutzov, Bojidar, Valentina Ganeva, Boyana Angelova, and Miguel Arevalo-Rodrigez. "Electroinduced release of recombinant proteins from Escherichia coli." New Biotechnology 33 (July 2016): S199. http://dx.doi.org/10.1016/j.nbt.2016.06.1407.

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32

Linton, Kenneth J., and Christopher F. Higgins. "The Escherichia coli ATP-binding cassette (ABC) proteins." Molecular Microbiology 28, no. 1 (2002): 5–13. http://dx.doi.org/10.1046/j.1365-2958.1998.00764.x.

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33

Riley, M. "Genes and proteins of Escherichia coli K-12." Nucleic Acids Research 26, no. 1 (1998): 54. http://dx.doi.org/10.1093/nar/26.1.54.

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34

Siegele, D. A., and L. J. Guynn. "Escherichia coli proteins synthesized during recovery from starvation." Journal of bacteriology 178, no. 21 (1996): 6352–56. http://dx.doi.org/10.1128/jb.178.21.6352-6356.1996.

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35

Lambert, L. A., K. Abshire, D. Blankenhorn, and J. L. Slonczewski. "Proteins induced in Escherichia coli by benzoic acid." Journal of bacteriology 179, no. 23 (1997): 7595–99. http://dx.doi.org/10.1128/jb.179.23.7595-7599.1997.

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36

Luirink, Joen, Zhong Yu, Samuel Wagner, and Jan-Willem de Gier. "Biogenesis of inner membrane proteins in Escherichia coli." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1817, no. 6 (2012): 965–76. http://dx.doi.org/10.1016/j.bbabio.2011.12.006.

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37

Smith, Austin E., Larry Z. Zhou, and Gary J. Pielak. "Hydrogen exchange of disordered proteins in Escherichia coli." Protein Science 24, no. 5 (2015): 706–13. http://dx.doi.org/10.1002/pro.2643.

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38

JACQUELÍN, Daniela K., Adrián FILIBERTI, Carlos E. ARGARAÑA, and José L. BARRA. "Pseudomonas aeruginosa MutL protein functions in Escherichia coli." Biochemical Journal 388, no. 3 (2005): 879–87. http://dx.doi.org/10.1042/bj20042073.

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Escherichia coli MutS, MutL and MutH proteins act sequentially in the MMRS (mismatch repair system). MutH directs the repair system to the newly synthesized strand due to its transient lack of Dam (DNA-adenine methylase) methylation. Although Pseudomonas aeruginosa does not have the corresponding E. coli MutH and Dam homologues, and consequently the MMRS seems to work differently, we show that the mutL gene from P. aeruginosa is capable of complementing a MutL-deficient strain of E. coli. MutL from P. aeruginosa has conserved 21 out of the 22 amino acids known to affect functioning of E. coli

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39

Wells, Timothy J., Makrina Totsika, and Mark A. Schembri. "Autotransporters of Escherichia coli: a sequence-based characterization." Microbiology 156, no. 8 (2010): 2459–69. http://dx.doi.org/10.1099/mic.0.039024-0.

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Autotransporter (AT) proteins are found in all Escherichia coli pathotypes and are often associated with virulence. In this study we took advantage of the large number of available E. coli genome sequences to perform an in-depth bioinformatic analysis of AT-encoding genes. Twenty-eight E. coli genome sequences were probed using an iterative approach, which revealed a total of 215 AT-encoding sequences that represented three major groups of distinct domain architecture: (i) serine protease AT proteins, (ii) trimeric AT adhesins and (iii) AIDA-I-type AT proteins. A number of subgroups were ident

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40

Liang, Ping, Bernard Labedan, and Monica Riley. "Physiological genomics of Escherichia coli protein families." Physiological Genomics 9, no. 1 (2002): 15–26. http://dx.doi.org/10.1152/physiolgenomics.00086.2001.

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The well-researched Escherichia coli genome offers the opportunity to explore the value of using protein families within a single organism to enrich functional annotation procedures and to study mechanisms of protein evolution. Having identified multimodular proteins resulting from gene fusion, and treated each module as a separate protein, nonoverlapping sequence-similar families in E. coli could be assembled. Of 3,902 proteins of length 100 residues or more, 2,415 clustered into 609 protein families. The relatedness of function among members of each family was dissected in detail. Data on pa

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41

Polo, Jesus, Angela Brijaldo, Maria Londoño, Diego Velasco, Jaime Cardozo, and Fabian Rueda. "Heterologous expression of bovine spermadhesin-1 using escherichia coli as biofactory." SPERMOVA 12, no. 1 (2022): 45–51. http://dx.doi.org/10.18548/aspe/0010.08.

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Seminal plasma proteins (SPP) are fundamental for oocyte fertilization by sperm cells. In bovine, the structure and function of SPP have been widely described in several studies, where the spermadhesin family has been highlighted. Spermadhesin proteins are closely related to sperm motility and viability along with protecting the sperm cells against oxidative stress. Spermadhesin-1, also known as acidic Seminal Fluid Proteins (aSFP), exhibits a redox activity that protects the sperm cells from reactive oxygen species (ROS), an important feature that could be taken in advantage to improve the po

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42

Peng, Xiao-Pei, Wei Ding, Jian-Min Ma, et al. "Effect of Escherichia Coli Infection on Metabolism of Dietary Protein in Intestine." Current Protein & Peptide Science 21, no. 8 (2020): 772–76. http://dx.doi.org/10.2174/1389203720666191113144049.

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Dietary proteins are linked to the pathogenic Escherichia coli (E. coli) through the intestinal tract, which is the site where both dietary proteins are metabolized and pathogenic E. coli strains play a pathogenic role. Dietary proteins are degraded by enzymes in the intestine lumen and their metabolites are transferred into enterocytes to be further metabolized. Seven diarrheagenic E. coli pathotypes have been identified, and they damage the intestinal epithelium through physical injury and effector proteins, which lead to inhibit the digestibility and absorption of dietary proteins in the in

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43

Uozumi, Nobuyuki. "Escherichia colias an expression system for K+transport systems from plants." American Journal of Physiology-Cell Physiology 281, no. 3 (2001): C733—C739. http://dx.doi.org/10.1152/ajpcell.2001.281.3.c733.

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The value of the Escherichia coli expression system has long been established because of its effectiveness in characterizing the structure and function of exogenously expressed proteins. When eukaryotic membrane proteins are functionally expressed in E. coli, this organism can serve as an alternative to eukaryotic host cells. A few examples have been reported of functional expression of animal and plant membrane proteins in E. coli. This mini-review describes the following findings: 1) homologous K+transporters exist in prokaryotic cells and in eukaryotic cells; 2) plant K+transporters can fun

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44

Silva, Liliana S. O., Pedro M. Matias, Célia V. Romão, and Lígia M. Saraiva. "Repair of Iron Center Proteins—A Different Class of Hemerythrin-Like Proteins." Molecules 27, no. 13 (2022): 4051. http://dx.doi.org/10.3390/molecules27134051.

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Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on Escherichia coli RIC (also known as YtfE), which remains the best-studied protein with extensive

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45

Kwon, Soon-Bok, Yun-A. Jung, and Dong-Bin Lim. "Proteomic analysis of heat-stable proteins in Escherichia coli." BMB Reports 41, no. 2 (2008): 108–11. http://dx.doi.org/10.5483/bmbrep.2008.41.2.108.

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46

Adamowicz, M., P. M. Kelley, and K. W. Nickerson. "Detergent (sodium dodecyl sulfate) shock proteins in Escherichia coli." Journal of Bacteriology 173, no. 1 (1991): 229–33. http://dx.doi.org/10.1128/jb.173.1.229-233.1991.

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47

Liu, Chang C., and Peter G. Schultz. "Recombinant expression of selectively sulfated proteins in Escherichia coli." Nature Biotechnology 24, no. 11 (2006): 1436–40. http://dx.doi.org/10.1038/nbt1254.

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48

Guerrero-Barrera, A. L., C. M. Garcia-Cuellar, J. D. Villalba, et al. "Actin-related proteins in Anabaena spp. and Escherichia coli." Microbiology 142, no. 5 (1996): 1133–40. http://dx.doi.org/10.1099/13500872-142-5-1133.

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49

Ward, A., J. O'Reilly, N. G. Rutherford, et al. "Expression of prokaryotic membrane transport proteins in Escherichia coli." Biochemical Society Transactions 27, no. 6 (1999): 893–99. http://dx.doi.org/10.1042/bst0270893.

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50

Sakellaris, Harry, Donna P. Balding, and June R. Scott. "Assembly proteins of CS1 pili of enterotoxigenic Escherichia coli." Molecular Microbiology 21, no. 3 (1996): 529–41. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02562.x.

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