Related ArticlesA preliminary CD and NMR study of the Escherichia coli DNA polymerase III theta subunit.
Proteins. 1999 Jul 1;36(1):111-6
Authors: Li D, Allen DL, Harvey S, Perrino FW, Schaaper RM, London RE
The theta subunit of DNA polymerase III, the main replicative polymerase of Escherichia coli, has been examined by circular dichroism and by NMR spectroscopy. The polymerase core consists of three subunits: alpha, epsilon, and theta, with alpha possessing the polymerase activity, epsilon functioning as a proofreading exonuclease, and theta, a small subunit of 8.9 kD, of undetermined function. The theta subunit has been expressed in E. coli, and a CD analysis of theta indicates the presence of a significant amount of secondary structure: approximately 52% alpha helix, 9% beta sheet, 21% turns, and 18% random coil. However, at higher concentrations, theta yields a poorly-resolved 1D proton NMR spectrum in which both the amide protons and the methyl protons show poor chemical shift dispersion. Subsequent 1H-15N HSQC analysis of uniformly-15N-labeled theta supports the conclusion that approximately half of the protein is reasonably well-structured. Another quarter of the protein, probably including some of the N-terminal region, is highly mobile, exhibiting a chemical shift pattern indicative of random coil structure. The remaining amide resonances exhibit significant broadening, indicative of intermolecular and/or intramolecular exchange processes. Improved chemical shift dispersion and greater uniformity of resonance intensities in the 1H-15N HSQC spectra resulted when [U-15N]-theta was examined in the presence of epsilon186--the N-terminal domain of the epsilon-subunit. Further work is currently in progress to define the solution structure of theta and the theta-epsilon186 complex.
[NMR paper] Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase
Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy.
Related Articles Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy.
Biochemistry. 2003 Apr 8;42(13):3635-44
Authors: DeRose EF, Darden T, Harvey S, Gabel S, Perrino FW, Schaaper RM, London RE
The DNA polymerase III holoenzyme (HE) is the primary replicative polymerase of Escherichia coli. The epsilon (epsilon) subunit of HE provides the 3'-->5' exonucleolytic proofreading...
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[NMR paper] NMR solution structure of the theta subunit of DNA polymerase III from Escherichia co
NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
Related Articles NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
Protein Sci. 2000 Apr;9(4):721-33
Authors: Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE
The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits (alpha, epsilon, and theta). The theta subunit is the smallest, but the least understood of the three. As a first step in a program aimed at understanding its...
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[NMR paper] Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
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Biol Pharm Bull. 1993 May;16(5):437-43
Authors: Shindo H, Kurumizaka H, Furubayashi A, Sakuma C, Matsumoto U, Yanagida A, Goshima N, Kano Y, Imamoto F
It was confirmed that the flexible arm region of HU alpha forms an antiparallel beta-sheet and that all of the residues of phenylalanines, together with some of...
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[NMR paper] 1H NMR study of the solution molecular and electronic structure of Escherichia coli f
1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
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Biochemistry. 1991 Feb 26;30(8):2156-65
Authors: Wu JZ, La Mar GN, Yu LP, Lee KB, Walker FA, Chiu ML, Sligar SG
The solution 500-MHz 1H NMR...
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
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Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Related Articles 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
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[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
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Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
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[NMR paper] NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu
NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Related Articles NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain.
Biochemistry. 1991 Nov 12;30(45):10872-7
Authors: Lowry DF, Cool RH, Redfield AG, Parmeggiani A
The phosphoryl-binding elements in the GDP-binding domain of elongation factor Tu were studied by heteronuclear proton observe methods. Five proton resonances were found below 10.5 ppm. Two of these were assigned to the amide...
A preliminary CD and NMR study of the Escherichia coli DNA polymerase III theta subun
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