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Defective Assembly of the Small Ribosomal Subunit in a Temperature-Sensitive Mutant of Escherichia coli. Experiments in vitro
| Content Provider | Scilit |
|---|---|
| Author | Hayes, Françoise Schmitt, Sophie |
| Copyright Year | 1980 |
| Description | Journal: Journal of Biological Inorganic Chemistry Comparison of the properties in vitro of total 30-S ribosomal subunit proteins and purified protein S4 of Escherichia coli D10 (wild type) and E. coli 219ts2(temperature-sensitive) has given the following results. 1. Reconstitution of functional 30-S subunits in vitro occurs when total 30-S subunit proteins of either strain are used even at temperatures which are not permissive for 30-S subunit assembly in vivo in E. coli 219ts2. The yield of reconstitution is, however, twofold lower with 30-S subunit proteins of E. coli 219ts2 than with wild-type proteins. 2. The yield of complex formation between 16-S rRNA and protein S4 of E. coli 219ts2 is temperature-sensitive and lower at all temperatures tested (33-42 degrees C) than that observed when wild-type S4 is used. 3. The conformational stability of complexes between 16-S rRNA and S4 from 219ts2 is more temperature-sensitive than that of analogous complexes containing wild-type S4. These observations provide an explanation for the temperature sensitivity of 30-S subunit assembly in E. coli 219ts2. |
| Ending Page | 103 |
| Starting Page | 95 |
| ISSN | 2573508X |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1980.tb04629.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 1 |
| Volume Number | 107 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1980-06-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Escherichia Coli Ribosomal Subunit Small Ribosomal Sensitive Mutant Defective Assembly |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |