دورية أكاديمية
Cold shock and its effect on ribosomes and thermal tolerance in Listeria monocytogenes.
| العنوان: | Cold shock and its effect on ribosomes and thermal tolerance in Listeria monocytogenes. |
|---|---|
| المؤلفون: | Bayles DO; Eastern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, Wyndmoor, Pennsylvania 19038, USA. dbayles@arserrc.gov, Tunick MH, Foglia TA, Miller AJ |
| المصدر: | Applied and environmental microbiology [Appl Environ Microbiol] 2000 Oct; Vol. 66 (10), pp. 4351-5. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 7605801 Publication Model: Print Cited Medium: Print ISSN: 0099-2240 (Print) Linking ISSN: 00992240 NLM ISO Abbreviation: Appl Environ Microbiol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Society for Microbiology. |
| مواضيع طبية MeSH: | Cold Temperature*, Listeria monocytogenes/*physiology , Ribosomes/*physiology, Calorimetry, Differential Scanning ; Fatty Acids/metabolism ; Hot Temperature ; Intracellular Membranes/physiology ; Listeria monocytogenes/genetics ; Listeria monocytogenes/ultrastructure ; Membrane Lipids/metabolism ; Protein Biosynthesis ; Ribosomes/genetics ; Ribosomes/ultrastructure ; Thermodynamics |
| مستخلص: | Differential scanning calorimetry (DSC) and fatty acid analysis were used to determine how cold shocking reduces the thermal stability of Listeria monocytogenes. Additionally, antibiotics that can elicit production of cold or heat shock proteins were used to determine the effect of translation blockage on ribosome thermal stability. Fatty acid profiles showed no significant variations as a result of cold shock, indicating that changes in membrane fatty acids were not responsible for the cold shock-induced reduction in thermal tolerance. Following a 3-h cold shock from 37 to 0 degrees C, the maximum denaturation temperature of the 50S ribosomal subunit and 70S ribosomal particle peak was reduced from 73.4 +/- 0.1 degrees C (mean +/- standard deviation) to 72.1 +/- 0.5 degrees C (P < or = 0.05), indicating that cold shock induced instability in the associated ribosome structure. The maximum denaturation temperature of the 30S ribosomal subunit peak did not show a significant shift in temperature (from 67.5 +/- 0.4 degrees C to 66.8 +/- 0.5 degrees C) as a result of cold shock, suggesting that either 50S subunit or 70S particle sensitivity was responsible for the intact ribosome fragility. Antibiotics that elicited changes in maximum denaturation temperature in ribosomal components also elicited reductions in thermotolerance. Together, these data suggest that ribosomal changes resulting from cold shock may be responsible for the decrease in D value observed when L. monocytogenes is cold shocked. |
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| المشرفين على المادة: | 0 (Fatty Acids) 0 (Membrane Lipids) |
| تواريخ الأحداث: | Date Created: 20000930 Date Completed: 20001130 Latest Revision: 20210526 |
| رمز التحديث: | 20240627 |
| مُعرف محوري في PubMed: | PMC92307 |
| DOI: | 10.1128/AEM.66.10.4351-4355.2000 |
| PMID: | 11010881 |
| قاعدة البيانات: | MEDLINE |
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