## Abstract Die normale Zellteilung der Mutante __ts__ 33‐6 von __Bacillus subtilis__ SB 19 bei 30 °C und das filamentöse Wachstum bei 46 °C werden von charakteristischen Aktivitätsunterschieden der Aminoacyl‐tRNS Synthetasen (AAS) begleitet. Diese in früheren Arbeiten vorgestellten allgemeinen Wec
Wechselwirkungen zwischen Aminoacyl-tRNS Synthetasen (AAS) und Zellteilung bei einer temperatursensitiven filamentösen Mutante von Bacillus subtilis SB 19 III. Charakterisierung des Vorinkubationseffektes und Einfluß eines AAS-Inhibitors aus Agrostemma githago-Keimlingen
✍ Scribed by Dr. J. Süss; M. Hecker
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 591 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
Further results on the correlations between the regulation of bacterial cell division and aminoacyl‐tRNA synthetase are presented. Activity of aminoacyl‐tRNA synthetases, extracted from a filamentous mutant of Bacillus subtilis SB 19, may be stimulated by preincubation of crude extracts.
The mechanism of this stimulating effect has been studied by means of an inhibitor of aminoacyl‐tRNA synthetases produced during the growth of Agrostemma githago‐seedlings. According to preliminary results we suggest, this inhibitor can reduce the activity of subunits only, but not that of higher associates. Association of subunits to oligomers will be prevented by the inhibitor, too. Our results may be indicative of the assumption that the increase of enzyme activity during preincubation of bacterial extracts, eliminated by the inhibitor, is changed by the association of subunits with a low catalytic activity to functional oligomers.
As to the verification of these hypotheses further work will still have to be done.
📜 SIMILAR VOLUMES
## Abstract Die temperatursensitive filamentöse Mutante __ts__ 33‐6 von __B. subtilis__ SB 19 zeichnet sich durch unterschiedliches Teilungsvermögen bei restriktiver und permissiver Temperatur aus (30 °C Kurzstäbchen, 46 °C Filamente), das von charakteristischen Aktivitätswechseln der Aminoacyl‐tRN