Hypersensitivity of Rhodobacter sphaeroides ribosomes to protein synthesis inhibitors: structural and functional implications

1994 ◽  
Vol 40 (9) ◽  
pp. 699-704 ◽  
Author(s):  
E. Sánchez ◽  
J. Teixidó ◽  
R. Guerrero ◽  
R. Amils

The elongation cycle of protein synthesis systems of purple nonsulfur photosynthetic bacteria Rhodobacter sphaeroides, grown both phototrophically and chemotrophically, was studied using 33 inhibitors with different chemical structures and functional and domain specificities. No functional differences between phototrophic and chemotrophic ribosomal systems were detected. Rhodobacter sphaeroides ribosomes exhibited strong hypersensitivity to nine functional inhibitors when compared with Escherichia coli ribosomes. Most of the R. sphaeroides ribosomal hypersensitivities corresponded to peptidyltransferase inhibitors, implying that this important functional neighborhood must be somehow different in the two organisms.Key words: protein synthesis inhibitors, ribosomal function, peptidyltransferase, photosynthetic bacteria.

2014 ◽  
Vol 3 (1) ◽  
pp. 63-68
Author(s):  
Meredith Joy Reesor ◽  
Isaac Joseph King ◽  
Jeffrey Copeland

Multidrug resistance bacteria pose a significant threat to human health and the efforts of the medical community.  Given our reliance on antibiotics for therapeutic treatment of bacterial infections it is imperative to understand the mechanism by which bacteria develop antibiotic resistance.  In the present report we develop a strain of Escherichia coli capable of resisting high levels of tetracycline and other protein synthesis inhibitors.  Furthermore the tetracycline resistant strain is approximately 1/3rd in length and is sensitive to UV radiation.


1974 ◽  
Vol 249 (19) ◽  
pp. 6280-6287 ◽  
Author(s):  
Kathleen Crist Westover ◽  
Lewis A. Jacobson

Author(s):  
Cecilia Valencia ◽  
Felipe Alonso Pérez ◽  
Carola Matus ◽  
Ricardo Felmer ◽  
María Elena Arias

Abstract The present study evaluated the mechanism by which protein synthesis inhibitors activate bovine oocytes. The aim was to analyze the dynamics of MPF and MAPKs. MII oocytes were activated with ionomycin (Io), ionomycin+anisomycin (ANY) and ionomycin+cycloheximide (CHX) and by in vitro fertilization (IVF). The expression of cyclin B1, p-CDK1, p-ERK1/2, p-JNK, and p-P38 were evaluated by immunodetection and the kinase activity of ERK1/2 was measured by enzyme assay. Evaluations at 1, 4, and 15 hours postactivation (hpa) showed that the expression of cyclin B1 was not modified by the treatments. ANY inactivated MPF by p-CDK1Thr14-Tyr15 at 4 hpa (P < 0.05), CHX increased pre-MPF (p-CDK1Thr161 and p-CDK1Thr14-Tyr15) at 1 hpa and IVF increased p-CDK1Thr14-Tyr15 at 17 hours postfertilization (hpf) (P < 0.05). ANY and CHX reduced the levels of p-ERK1/2 at 4 hpa (P < 0.05) and its activity at 4 and 1 hpa, respectively (P < 0.05). Meanwhile, IVF increased p-ERK1/2 at 6 hpf (P < 0.05); however, its kinase activity decreased at 6 hpf (P < 0.05). p-JNK in ANY, CHX, and IVF oocytes decreased at 4 hpa (P < 0.05). p-P38 was only observed at 1 hpa, with no differences between treatments. In conclusion, activation of bovine oocytes by ANY, CHX, and IVF inactivates MPF by CDK1-dependent specific phosphorylation without cyclin B1 degradation. ANY or CHX promoted this inactivation, which seemed to be more delayed in the physiological activation (IVF). Both inhibitors modulated MPF activity via an ERK1/2-independent pathway, whereas IVF activated the bovine oocytes via an ERK1/2-dependent pathway. Finally, ANY does not activate the JNK and P38 kinase pathways.


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