Control of ribosome turnover during growth of the haloalkaliphilic archaeon Natronococcus occultus
✍ Scribed by Débora Nercessian; Rubén D. Conde
- Book ID
- 116860296
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 163 KB
- Volume
- 157
- Category
- Article
- ISSN
- 0923-2508
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Intracellular proteolytic activity was detected in the haloalkaliphilic archaeon Natronococcus occultus during the stationary phase of cultures grown in complete medium and during carbon and nitrogen starvation. Puromycin prevented the occurrence of proteolytic activity in starved cells, suggesting
A serine protease was purified from Natronococcus occultus stationary phase culture medium (328-fold, yield 19%) and characterized at the biochemical level. The enzyme has a native molecular mass of 130 kDa, has chymotrypsin-like activity, is stable and active in a broad pH range (5.5 -12), is rathe