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Production of abnormal proteins in E. coli stimulates transcription of ion and other heat shock genes
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Protein turnover: Intracellular protein degradation
2021, Encyclopedia of Biological Chemistry: Third EditionThe biology of Lonp1: More than a mitochondrial protease
2020, International Review of Cell and Molecular BiologyCitation Excerpt :Concerning hypoxia, LONP1 is upregulated in THP-1 (monocytic cancer), HeLa (cervical cancer) and RKO (colon cancer) cells by low oxygen tension, through the binding of HIF-1α on the LONP1 promoter (Fukuda et al., 2007; Goto et al., 2014). Interestingly, LONP1 upregulation in humans cells is determined by stimuli that are strongly preserved during evolution, such as the accumulation of abnormal proteins or heat shock, both already present in E. coli (Goff and Goldberg, 1985; Goff et al., 1984; Phillips et al., 1984). Our current understanding of LONP1 processing is that it is translated in the cytosol as a mitochondrial precursor protein of 959 amino acids and a molecular mass of 106 kDa, which is then targeted to the mitochondrial outer membrane by its amino-terminal MTS (Fig. 1A).
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2015, BiomaterialsCitation Excerpt :Extracellular Strep (A) is allocated to each cell in accordance with influx and efflux rates, and binds to ribosomes (RsA), leading to inhibition of protein synthesis and ultimately cell death [38]. Strep can also cause heat shock response (HSR) due to translational errors [39,40], which will further degrade the ribosomal RNA and proteins [41]. HSR is also critical for generation of IE by this mechanism [35]: for an intermediate antibiotic concentration, a population with a high initial density can survive but one with a low initial density cannot.