Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease
| العنوان: | Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease |
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| المؤلفون: | Gracjana Klein, Daria Biernacka, Satish Raina, Patrycja Gorzelak |
| المصدر: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 21, Iss 9088, p 9088 (2020) Volume 21 Issue 23 |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Lipopolysaccharides, Threonine, Transcription, Genetic, medicine.medical_treatment, Mutant, Amino Acid Motifs, LapB, LapC, urologic and male genital diseases, Hydroxamic Acids, lcsh:Chemistry, Suppression, Genetic, ATP-Dependent Proteases, Transcription (biology), Promoter Regions, Genetic, lcsh:QH301-705.5, Spectroscopy, Conserved Sequence, Heat-Shock Proteins, Phospholipids, medicine.diagnostic_test, biology, YejM, Chemistry, Escherichia coli Proteins, lipopolysaccharide, Temperature, General Medicine, Computer Science Applications, Cell biology, FabZ, Essential gene, Periplasm, HslV/U protease, Proteolysis, Protein subunit, 030106 microbiology, HslVU, Catalysis, Article, LpxC, Amidohydrolases, Inorganic Chemistry, 03 medical and health sciences, Protein Domains, Operon, medicine, Escherichia coli, Amino Acid Sequence, Physical and Theoretical Chemistry, Molecular Biology, Suppressor mutation, Protease, RpoE, Organic Chemistry, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Mutation, biology.protein, Biocatalysis |
| الوصف: | We previously showed that lipopolysaccharide (LPS) assembly requires the essential LapB protein to regulate FtsH-mediated proteolysis of LpxC protein that catalyzes the first committed step in the LPS synthesis. To further understand the essential function of LapB and its role in LpxC turnover, multicopy suppressors of &Delta lapB revealed that overproduction of HslV protease subunit prevents its lethality by proteolytic degradation of LpxC, providing the first alternative pathway of LpxC degradation. Isolation and characterization of an extragenic suppressor mutation that prevents lethality of &Delta lapB by restoration of normal LPS synthesis identified a frame-shift mutation after 377 aa in the essential gene designated lapC, suggesting LapB and LapC act antagonistically. The same lapC gene was identified during selection for mutations that induce transcription from LPS defects-responsive rpoEP3 promoter, confer sensitivity to LpxC inhibitor CHIR090 and a temperature-sensitive phenotype. Suppressors of lapC mutants that restored growth at elevated temperatures mapped to lapA/lapB, lpxC and ftsH genes. Such suppressor mutations restored normal levels of LPS and prevented proteolysis of LpxC in lapC mutants. Interestingly, a lapC deletion could be constructed in strains either overproducing LpxC or in the absence of LapB, revealing that FtsH, LapB and LapC together regulate LPS synthesis by controlling LpxC amounts. |
| وصف الملف: | application/pdf |
| تدمد: | 1422-0067 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df0ed45e17ebc48ebfc1ed21677b9d4f https://pubmed.ncbi.nlm.nih.gov/33260377 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....df0ed45e17ebc48ebfc1ed21677b9d4f |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14220067 |
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