Escherichia coli RNase D. Catalytic properties and substrate specificity.
نویسندگان
چکیده
منابع مشابه
Probing the substrate specificity of Escherichia coli RNase E using a novel oligonucleotide-based assay.
Endoribonuclease RNase E has a central role in both processing and decay of RNA in Escherichia coli, and apparently in many other organisms, where RNase E homologs were identified or their existence has been predicted from genomic data. Although the biochemical properties of this enzyme have been already studied for many years, the substrate specificity of RNase E is still poorly characterized....
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A multiple mutant strain of Escherichia coli containing mutations affecting the exoribonucleases, RNase II, RNase D, and RNase BN, and also the endonuclease, RNase I, was constructed by P1-mediated transduction. Extracts of the mutant strain were lacking the aforementioned RNase activities. The multiple mutant displayed normal growth in both rich and minimal media at a variety of temperatures, ...
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Purified preparations from Escherichia coli of the enzyme thymidine :orthophosphate deoxyribosyltransferase (EC 2.4. 2.4) or thymidine phosphorylase are specific for deoxyribose lphosphate. A number of pyrimidine bases function in the reaction, however, including uracil, 5-bromoand 5-aminouracil, 2-thiothymine, and 2-thiouracil, whereas deoxycytidine is inert (1). The level of enzyme in extract...
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The small ribosome subunit of Escherichia coli contains 10 base-methylated sites distributed in important functional regions. At present, seven enzymes responsible for methylation of eight bases are known, but most of them have not been well characterized. One of these enzymes, RsmE, was recently identified and shown to specifically methylate U1498. Here we describe the enzymatic properties and...
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RNase E plays an essential role in RNA processing and decay and tethers to the cytoplasmic membrane in Escherichia coli; however, the function of this membrane-protein interaction has remained unclear. Here, we establish a mechanistic role for the RNase E-membrane interaction. The reconstituted highly conserved N-terminal fragment of RNase E (NRne, residues 1-499) binds specifically to anionic ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)69251-3