Escherichia coli subunits

Maeda, H., Fujita, N., and Ishihama, A. (2000) Competition among seven Escherichia coli subunits Relative binding affinities to the core RNA polymerase. Nucleic Acids Res. 28, 3497-3503. 

Wingfield, P. T., Stahl, S. J., Williams, R. W., and Steven, A. G. (1995). Hepatitis core antigen produced in Escherichia coli subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 34, 4919-4932. 

Each subunit of the homotetrameric PFK of Escherichia coli comprises 320 amino acids arranged in two domains, one large and one smaller, both of which have an rx/p structure reminiscent of the Rossman fold (Figure 6.25). 

Escherichia coli FiFg ATP Synthase Subunit Organization ... 

Fig. 6. Representative EPR spectra displayed by trinuclear and tetranucleEir iron-sulfur centers, (a) and (b) [3Fe-4S] + center in the NarH subunit of Escherichia coli nitrate reductase and the Ni-Fe hydrogenase fromD. gigas, respectively, (c) [4Fe-4S] + center in D. desulfuricans Norway ferredoxin I. (d) [4Fe-4S] center in Thiobacillus ferrooxidans ferredoxin. Experimental conditions temperature, 15 K microwave frequency, 9.330 GHz microwave power, (a) 100 mW, (b) 0.04 mW, (c) smd (d) 0.5 mW modulation amplitude (a), (c), (d) 0.5 mT, (b) 0.1 mT.

Anton DL, R Kutny (1987) Escherichia coli 5-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NHj-terminal sequences. J Biol Chem 262 2817-2822. 

Isolated polynucleotide clusters from Rhodococcus opacus which encode four polypeptides possessing the activities of a NHase (a and /3 subunits), an auxiliary protein P15K that activates the NHase, and a cobalt transporter protein were expressed in Escherichia coli DSM 14459 cells [34]. Methionine nitrile was added continuously to a suspension of the transformant cells (5.6% w/v of wet cells) in phosphate buffer (50 mM, pH 7.5) at 20 °C, at a rate where the nitrile concentration did not exceed 15 g L 1 while maintaining the pH constant at 7.5. After 320 min, the nitrile was completely converted into amide, corresponding to a final product concentration of 176 gL1.4-Methylthio-a-hydroxybutyramide is readily hydrolyzed with calcium hydroxide, where the calcium salt of 4-methylthio-a-hydroxybutyric acid (MHA) can be directly used as a nutritional supplement in animal feed as an alternative to methionine or MHA. 

Bragg, P.D., and Hou, C. (1975) Subunit composition, function, and spatial arrangement in the Ca2+-and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimurium. Arch. Biochem. Biophys. 167, 311-321. 

Chang, F.N., and Flaks, J.C. (1972) Specific cross-linking of Escherichia coli 30S ribosomal subunit. J. Mol. Biol. 68, 177. 

Cover, J.A., Lambert, J.M., Norman, C.M., and Traut, R.R. (1981) Identification of proteins at the subunit interface of the Escherichia coli ribosome by cross-linking with dimethyl 3,3 -dithiobis(propionimi date). Biochemistry 20, 2843-2852. 

Czworkowski, J., Odom, O.W., and Hardesty, B. (1991) Study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli. Biochemistry 30, 4821. 

Freedberg, W.B., and Hardman, J.K. (1971) Structural and functional roles of the cysteine residues in the a-subunit of the Escherichia coli tryptophan synthetase./. Biol. Chem. 246, 1439. 

Greiner, D.P., Hughes, K.A., Gunasekera, A.H., and Meares, C.F. (1996) Binding of the sigma-70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting. Proc. Natl. Acad. Sci. USA 93, 71-75. 

Hillel, Z., and Wu, C.W. (1977) Subunit topography of RNA polymerase from Escherichia coli. A cross-linking study with bifunctional reagents. Biochemistry 16, 3334-3342. 

Miyake, R., Murakami, K., Owens, J.T., Greiner, D.P., Ozoline, O.N., Ishihama, A., and Meares, C.F. (1998) Dimeric association of Escherichia coli RNA polymerase alpha subunits, studied by cleavage of single-cysteine alpha subunits conjugated to iron-(S)-l-[p-(bromoacetamido)benzyl]ethylenediaminetet raacetate. Biochemistry 37(5), 1344-1349. 

Sun, T.T., Bollen, A., Kahan, L., and Traut, R.R. (1974) Topography of ribosomal proteins of the Escherichia coli 30S subunit as studied with the reversible cross-linking reagent methyl 4-mercaptobu-tyrimidate. Biochemistry 13, 2334—2340. 

To establish whether rifaximin, like the other members of the rifamycin family [36, 58], specifically inhibits bacterial RNA synthesis the effect of this antibiotic as well as that of rifampicin and chloramphenicol on RNA (via 3H-uridine incorporation), DNA (via 3H-thymidine incorporation) and protein (via 35S-methionine incorporation) synthesis was studied in growing cultures of Escherichia coli [59], While chloramphenicol reduced protein synthesis, both rifaximin and rifampicin inhibited RNA synthesis in a concentration-dependent fashion. In contrast, none of them affected 3H-thymidine incorporation into DNA. These data suggest that rifaximin, like rifampicin, inhibits RNA synthesis by binding the (3 subunit of the bacterial DNA-dependent RNA polymerase [60],... 

N. Drapal, A. Bock (1998) Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry, 37 2941-2948... 

E. Theodoratou, A. Paschos, S. Mintz-Weber, A. Bock (2000) Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli. Arch. Microbiol., 173 110-116... 

A comprehensive study of KDO 8-phosphate synthetase has been reported by Ray.137 The author purified the enzyme 450-fold from crude extracts of Escherichia coli B cells. The synthetase has a molecular mass of 90,000 6,000 daltons and is composed of three identical subunits having an apparent molecular mass of32,000 4,000 daltons. Two pH optima were observed, one being at pH 4.0-6.0 in succinate buffer, and the other, at pH 9.0 in glycine buffer. The isoelectric point of the enzyme is 5.1. The enzyme has an apparent KM for D-arabinose 5-phosphate of 20 pM and an apparent KM for enolpyruvate phosphate of 6 pM. 

Bogyo, M. et al. Covalent modification of the active site threonine of proteasomal f3 subunits and the Escherichia coli homolg HsIV by a new class of inhibitors. Proc. Natl. Acad. 

Bogyo, M., McMaster, J. S., Gaczinska, M., Toetoeelia, D., Goldberg, A. L., and Ploegh, H. Covalent modification of the active site threonine of proteasomal p-subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Nat. Acad. Sci. USA 1997, 94, 6629-6634. 

M. C., Yu, C. H., Lin, P. I., and Wu, W. F. Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system. /. Bacteriol. 2003, 185, 2393-2401. 

SwAMY, K. H. S., Chin, H. C., and Goldberg, A. L. Isolation and Characterization of Protease Do From Escherichia-Coli, a Large Serine Protease Containing Multiple Subunits. Arch. Biochem. Biophys. 1983, 224, 543-554. 

D Arcy A, Stihle M, Kostrewa D, Dale G. 1999. Crystal engineering a case study using the 24 kDa fragment of the DNA Gyrase B subunit from Escherichia Coli. Acta Cryst D55 1623-1625. 

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