Results 261 to 270 of about 299,739 (289)

Equilibrium unfolding of RNase Rs from Rhizopus stolonifer: pH dependence of chemical and thermal denaturation

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The conformational stability of RNase Rs was determined with chemical and thermal denaturants over the pH range of 1-10. Equilibrium unfolding with urea showed that values of D(1/2) (5.7 M) and DeltaG(H(2)O) (12.8 kcal/mol) were highest at pH 5.0, its pI and the maximum conformational stability of RNase Rs was observed near pH 5.0.
Rajashree A. Deshpande, M. Islam Khan, Vepatu Shankar   +2 more
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The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

Cancer Letters, 2006
TCL1 is an AKT kinase coactivator that, when dysregulated, initiates mature lymphocyte malignancies in humans and transgenic mice. While TCL1 augments AKT pathway signaling, additional TCL1 interacting proteins that may contribute to cellular homeostasis or transformation are lacking.
Samuel W. French, David W. Dawson, Hsiao‐Wen Chen, Robert N. Rainey, Stuart A. Sievers, Cynthia E. Balatoni, Larry Wong, Joshua J. Troke, Mai Nguyen, Carla M. Koehler, Michael A. Teitell   +10 more
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The pH-dependence of the Escherichia coli RNase HII-catalysed Reaction Suggests that an Active Site Carboxylate Group Participates Directly in Catalysis

Journal of Molecular Biology, 2007
RNase HII specifically catalyses the hydrolysis of phosphate diester linkages contained within the RNA portion of DNA/RNA hybrids. The catalytic parameters of the enzyme derived from Escherichia coli BL21 have been measured using 5'-fluorescent oligodeoxynucleotide substrates containing embedded ribonucleotides.
James A. Bastock, Michelle Webb, Jane A. Grasby   +2 more
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Processing yeast to reduce its nucleic acid content. Induction of intracellular RNase action by a simple heat‐shock procedure, and an efficient chemical method based on extraction of RNA by salt solutions at low pH

Journal of the Science of Food and Agriculture, 1978
AbstractAutolytic breakdown of the RNA of Saccharomyces cerevisiae can be induced by subjecting a suspension of yeast in NaCl solution at pH 6 to heat shock, produced by bringing the suspension to 50°C and then adding enough water at 100°C to increase the temperature momentarily to 68°C, followed after 1 min by the addition of cold water to reduce it ...
William E. Trevelyan
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Structure of theMethanothermobacter thermautotrophicusexosome RNase PH ring

Acta Crystallographica Section D Biological Crystallography, 2010
The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial polynucleotide phosphorylase (PNPase). While all six RNase PH monomers are catalytically active in the
Alfred A. Antson, Miguel Ortiz-Lombardía, Chyan Leong Ng, David G. Waterman   +3 more
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Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation

European Biophysics Journal, 2011
Equilibrium unfolding of A. niger RNase with chemical denaturants, for example GuHCl and urea, and thermal unfolding have been studied as a function of pH using fluorescence, far-UV, near-UV, and absorbance spectroscopy. Because of their ability to affect electrostatic interactions, pH and chemical denaturants have a marked effect on the stability ...
Anurag Sharma, Medicherla V. Jagannadham, Moni Kumari, Mira Debnath, Gundampati Ravi Kumar   +4 more
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pH Profile of Kinetic Constants of RNase Rh from Rhizopus niveus and Its Mutant Enzymes towards UpU, and Possible Mechanisms of RNase Rh

The Journal of Biochemistry, 1994
In order to elucidate the mechanism of action of Rhizopus niveus RNase Rh, we investigated the pH profiles of the kinetic parameters of RNase RNAP Rh, a derivative of RNase Rh, and its mutant enzymes, i.e., RNase RNAP Rh H104F, RNase RNAP Rh E105Q, and RNase RNAP Rh D51N. Based on comparisons of their profiles we concluded that protonation of His104 is
Hideaki Watanabe, Masachika Irie, Hiroyuki Horiuchi, Hiroyuki Kurihara, Kazuo T. Nakamura, Yukio Mitsui, Takamasa Nonaka, Masamichi Takagi, Kazuko Ohgi, Masanori Iwama   +9 more
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Cleavage Site Selection by M1 RNA, the Catalytic Subunit of Escherichia coli RNase P, is influenced by pH

Journal of Molecular Biology, 1994
We have studied cleavage site selection by M1 RNA, the catalytic subunit of Escherichia coli RNase P, under various reaction conditions using tRNA precursors which are cleaved at two positions. Our results showed that the preference of cleavage site changed with variations in pH or Mg2+ concentration.
Leif A. Kirsebom, Joanna Kufel
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Atomic resolution structures of rnase A at six ph values

2002
The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-
SICA, FILOMENA, MAZZARELLA, LELIO, ZAGARI, ADRIANA, LAMZIN V. S., WILSON K. S., BERISIO R.   +5 more
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Maturation of 23S rRNA in B.subtilis by RNaseJ1 and the 3'-5'-exoribonucleases RNase PH and YhaM in the absence of Mini-III

, 2010
Y. Redko, C. Condon
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