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Intracellular proteolytic activity of the haloalkaliphilic archaeon Natronococcus occultus. Effect of starvation

โœ Scribed by Karina Herrera Seitz; Claudia Studdert; Jorge Sanchez; Dr. Rosana de Castro


Book ID
102911680
Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
696 KB
Volume
37
Category
Article
ISSN
0233-111X

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โœฆ Synopsis


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 that de novo synthesis of proteolytic enzymes might be required for protein degradation during starvation. Intracellular proteolytic activity degraded casein and gelatin. It had a temperature optimum of 60 "C in 2 M NaCl and depended on high salt concentration (NaCl or KCl) for activity and stability. Gelatin zymography of cell extracts from stationary phase or starved cells showed a complex pattern of proteolytic bands ranging from -20 to 120 kDa. All these proteolytic bands were inhibited by PMSF') and chymostatin. However, they showed differences in stability to temperature and salt concentration. I ) Abbreviations: PMSF (phenylmethylsulphonyl fluoride); YE (yeast extract); TCA (trichloroacetic acid)


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Purification and biochemical characteriz
โœ Claudia Alicia Studdert; Maria Karina Herrera Seitz; Maria Ines Plasencia Gil; J ๐Ÿ“‚ Article ๐Ÿ“… 2001 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 93 KB ๐Ÿ‘ 1 views

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