A possible complex containing RNA processing enzymes
Autor: | Béla M. Prágai, David Apirion, Swatantra K. Jain |
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Rok vydání: | 1982 |
Předmět: |
Sucrose
Density gradient Cell Biophysics Biology medicine.disease_cause Biochemistry Ribosome chemistry.chemical_compound Ribonucleases Bacterial Proteins Centrifugation Density Gradient Escherichia coli medicine Centrifugation Molecular Biology chemistry.chemical_classification Strain (chemistry) Cell Biology Molecular biology medicine.anatomical_structure Enzyme chemistry RNA Ultracentrifugation |
Zdroj: | Biochemical and Biophysical Research Communications. 106:768-778 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(82)91777-6 |
Popis: | The three enzymes, RNAase III, RNAase E and RNAase P participate in the processing of RNA precursors in Escherichia coli . In extracts which contain a mutated RNAase III or RNAase E under certain conditions RNAase P activity is not expressed while in the wild-type extract it is. Upon high-speed centrifugation of a cell extract from a strain of E. , coli , which contains all these three enzymes, the majority of RNAase P, RNAase III and RNAase E activities sediment as particles heavier than their known sizes. In a sucrose density gradient of the cell extract, part of RNAase E and RNAase P activities co-sediment while most of the RNAase III activity is found toward the top of the gradient. This behavior is distinct from other ribonucleases such as RNAase II and RNAase H, which do not sediment as complexes. This complex does not seem to be caused merely by the association of the enzymes with ribosomes. |
Databáze: | OpenAIRE |
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