Nuclear Inheritance of Erythromycin Resistance in Human Cells: New Class of Mitochondrial Protein Synthesis Mutants

1982 ◽  
Vol 2 (6) ◽  
pp. 694-700
Author(s):  
Claus-Jens Doersen ◽  
Eric J. Stanbridge
Keyword(s):  
Protein Synthesis ◽  
Hela Cells ◽  
Mitochondrial Protein ◽  
Human Cells ◽  
Recessive Trait ◽  
Mitochondrial Protein Synthesis ◽  
Erythromycin Resistance ◽  
New Class ◽  
Resistant Mutants

The characterization of two new erythromycin-resistant mutants of HeLa cells is described. The strains ERY2305 and ERY2309 both exhibited resistance to erythromycin in growth assays and cell-free mitochondrial protein synthesis assays. The erythromycin resistance phenotype could not be transferred by cybridization. The mutation appeared to be encoded in the nucleus and inherited as a recessive trait. These two mutants, therefore, represent a new class of erythromycin-resistant mutants in human cells that is distinct from the cytoplasmically inherited mutation in strain ERY2301 described previously.

scholarly journals Nuclear Inheritance of Erythromycin Resistance in Human Cells: New Class of Mitochondrial Protein Synthesis Mutants

1982 ◽  
Vol 2 (6) ◽  
pp. 694-700 ◽  
Author(s):  
Claus-Jens Doersen ◽  
Eric J. Stanbridge
Keyword(s):  
Protein Synthesis ◽  
Hela Cells ◽  
Mitochondrial Protein ◽  
Human Cells ◽  
Recessive Trait ◽  
Mitochondrial Protein Synthesis ◽  
Erythromycin Resistance ◽  
New Class ◽  
Resistant Mutants

The characterization of two new erythromycin-resistant mutants of HeLa cells is described. The strains ERY2305 and ERY2309 both exhibited resistance to erythromycin in growth assays and cell-free mitochondrial protein synthesis assays. The erythromycin resistance phenotype could not be transferred by cybridization. The mutation appeared to be encoded in the nucleus and inherited as a recessive trait. These two mutants, therefore, represent a new class of erythromycin-resistant mutants in human cells that is distinct from the cytoplasmically inherited mutation in strain ERY2301 described previously.

scholarly journals Differences in the products of mitochondrial protein synthesis in vivo in human and mouse cells and their potential use as markers for the mitochondrial genome in human–mouse cell hybrids

1974 ◽  
Vol 144 (1) ◽  
pp. 161-164 ◽  
Author(s):  
Alec Jeffreys ◽  
Ian Craig
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Detailed Comparison ◽  
Cell Types ◽  
Mouse Cell ◽  
Human Cells ◽  
Mitochondrial Protein Synthesis ◽  
Cell Hybrids ◽  
Different Cell Types

The proteins synthesized in the mitochondria of mouse and human cells grown in tissue culture were examined by electrophoresis in polyacrylamide gels. The proteins were labelled by incubating the cells in the presence of [35S]methionine and an inhibitor of cytoplasmic protein synthesis (emetine or cycloheximide). A detailed comparison between the labelled products of mouse and human mitochondrial protein synthesis was made possible by developing radioautograms after exposure to slab-electrophoresis gels. Patterns obtained for different cell types of the same species were extremely similar, whereas reproducible differences were observed on comparison of the profiles obtained for mouse and human cells. Four human–mouse somatic cell hybrids were examined, and in each one only components corresponding to mouse mitochondrially synthesized proteins were detected.

FK506 affects mitochondrial protein synthesis and oxygen consumption in human cells

2013 ◽  
Vol 29 (6) ◽  
pp. 407-414 ◽  
Author(s):  
María Palacín ◽  
Eliecer Coto ◽  
Laura Llobet ◽  
David Pacheu-Grau ◽  
Julio Montoya ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Oxygen Consumption ◽  
Mitochondrial Protein ◽  
Human Cells ◽  
Mitochondrial Protein Synthesis

scholarly journals EXPRESSION OF THE MITOCHONDRIAL GENOME IN HELA CELLS

1973 ◽  
Vol 56 (3) ◽  
pp. 819-831 ◽  
Author(s):  
Brian Storrie ◽  
Giuseppe Attardi
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Genome ◽  
Hela Cells ◽  
Mitochondrial Protein ◽  
Selective Inhibition ◽  
Mitochondrial Protein Synthesis ◽  
Cloning Efficiency ◽  
Cell Growth Inhibition ◽  
Progressive Loss ◽  
Two Generations

The effect of selective inhibition of mitochondrial protein synthesis by chloramphenicol at 40 or 200 µg/ml on the formation of mitochondria in HeLa cells was investigated. HeLa cells, under the conditions used in the present work, grow at a decreasing rate for at least four cell generations in the presence of 40 µg/ml chloramphenicol, and for two generations in the presence of 200 µg/ml chloramphenicol. The progressive cell growth inhibition which begins after 2 days of exposure of the cells to 40 µg/ml chloramphenicol is immediately or gradually reversible, upon removal of the drug, for periods up to at least 8 days of treatment, though there is a progressive loss of cloning efficiency. In cells which have been treated for 6–7 days with 40 or 200 µg/ml of chloramphenicol, mitochondrial protein synthesis occurs at a normal or near-normal rate 1 h after removal of the drug. Mitochondria increase normally in number and show a normal size and amount of cristae in the presence of either concentration of drug. However, in 4–5% of the mitochondrial profiles the cristae appear to be arranged in unusual, circular, looped or whorled configuration.

scholarly journals High resolution imaging of nascent mitochondrial protein synthesis in cultured human cells

2020 ◽  
Author(s):  
Matthew Zorkau ◽  
Christin A Albus ◽  
Rolando Berlinguer-Palmini ◽  
Zofia MA Chrzanowska-Lightowlers ◽  
Robert N. Lightowlers
Keyword(s):  
Protein Synthesis ◽  
Outer Membrane ◽  
Mitochondrial Protein ◽  
Human Cells ◽  
Mitochondrial Rna ◽  
Mitochondrial Protein Synthesis ◽  
Inner Mitochondrial Membrane ◽  
Rna Granules ◽  
Cultured Human Cells ◽  
Boundary Membrane

AbstractHuman mitochondria contain their own genome, mtDNA, that is expressed in the mitochondrial matrix. This genome encodes thirteen vital polypeptides that are components of the multi-subunit complexes that couple oxidative phosphorylation (OXPHOS). The inner mitochondrial membrane that houses these complexes comprises the inner boundary membrane that runs parallel to the outer membrane, infoldings that form the cristae membranes, and the cristae junctions that separate the two. It is in these cristae membranes that the OXPHOS complexes have been shown to reside in various species. The majority of the OXPHOS subunits are nuclear-encoded and must therefore be imported from the cytosol through the outer membrane at contact sites with the inner boundary membrane. As the mitochondrially-encoded components are also integral members of these complexes, where does nascent protein synthesis occur? Transcription, mRNA processing, maturation and at least part of the mitoribosome assembly process occur at the nucleoid and the spatially juxtaposed mitochondrial RNA granules, is protein synthesis also performed at the RNA granules close to these entities, or does it occur distal to these sites ? We have adapted a click chemistry based method, coupled with STED nanoscopy to address these questions. We report that in human cells in culture, within the limits of our methodology, the majority of mitochondrial protein synthesis occurs at the cristae membranes and is spatially separated from the sites of RNA processing and maturation.

Sign in / Sign up

Export Citation Format

Share Document