Association of
            <i>Escherichia coli</i>
            ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle

Herskovits, Anat A.; Bibi, Eitan

doi:10.1073/pnas.080077197

Cited by 79 publications

(76 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1B). As such, the proportion of membrane-associated ribosomes in H. volcanii is far more similar to that reported in eukaryal cells (ϳ60 -80%) (35,36) that what has been reported in Bacteria (ϳ5-10%) (37,38).…”

Section: In H Volcanii a Major Proportion Of Ribosomes Are Membranesupporting

confidence: 83%

In the Archaea Haloferax volcanii, Membrane Protein Biogenesis and Protein Synthesis Rates Are Affected by Decreased Ribosomal Binding to the Translocon

Ring

Eichler

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

In the haloarchaea Haloferax volcanii, ribosomes are found in the cytoplasm and membrane-bound at similar levels. Transformation of H. volcanii to express chimeras of the translocon components SecY and SecE fused to a cellulose-binding domain substantially decreased ribosomal membrane binding, relative to non-transformed cells, likely due to steric hindrance by the cellulose-binding domain. Treatment of cells with the polypeptide synthesis terminator puromycin, with or without low salt washes previously shown to prevent in vitro ribosomal membrane binding in halophilic archaea, did not lead to release of translocon-bound ribosomes, indicating that ribosome release is not directly related to the translation status of a given ribosome. Release was, however, achieved during cell starvation or stationary growth, pointing at a regulated manner of ribosomal release in H. volcanii. Decreased ribosomal binding selectively affected membrane protein levels, suggesting that membrane insertion occurs co-translationally in Archaea. In the presence of chimera-incorporating sterically hindered translocons, the reduced ability of ribosomes to bind in the transformed cells modulated protein synthesis rates over time, suggesting that these cells manage to compensate for the reduction in ribosome binding. Possible strategies for this compensation, such as a shift to a post-translational mode of membrane protein insertion or maintained ribosomal membrane-binding, are discussed.

show abstract

Section: In H Volcanii a Major Proportion Of Ribosomes Are Membranesupporting

confidence: 83%

In the Archaea Haloferax volcanii, Membrane Protein Biogenesis and Protein Synthesis Rates Are Affected by Decreased Ribosomal Binding to the Translocon

Ring

Eichler

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Previous studies of FtsY revealed the receptor interaction with membranebound ribosomes (Herskovits et al, 2002) and with the SecYEG translocase (Angelini et al, 2005), and showed how FtsY is regulated on the membrane by acidic lipids Braig et al, 2009;Erez et al, 2010;Parlitz et al, 2007). Other studies showed that FtsY plays a central role in vivo in ribosome targeting to the membrane (Herskovits and Bibi, 2000) and in the productive expression of IMPs Yosef et al, 2010). Taken together, it is generally accepted that FtsY functions as a membrane-associated protein, as has been shown recently (Mircheva et al, 2009).…”

Section: Introductionmentioning

confidence: 72%

Co-translational membrane association of the Escherichia coli SRP receptor

Bercovich-Kinori

Bibi

2015

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

The signal recognition particle (SRP) receptor is a major player in the pathway of membrane protein biogenesis in all organisms. The receptor functions as a membrane-bound entity but very little is known about its targeting to the membrane. Here, we demonstrate in vivo that the Escherichia coli SRP receptor targets the membrane co-translationally. This requires emergence from the ribosome of the four-helix-long N-domain of the receptor, of which only helices 2-4 are required for co-translational membrane attachment. The results also suggest that the targeting might be regulated co-translationally. Taken together, our in vivo studies shed light on the biogenesis of the SRP receptor and its hypothetical role in targeting ribosomes to the E. coli membrane.

show abstract

“…There is biochemical evidence that membrane-bound ribosomes in E. coli are completely devoid of any physical connection with the nucleoids (46). It was also shown by independent studies that freely diffusing mRNAs are localized close to the cell periphery, where they are translated by ribosomes (19,27,28).…”

Section: Discussionmentioning

confidence: 97%

Organization of Ribosomes and Nucleoids in Escherichia coli Cells during Growth and in Quiescence

Chai¹,

Singh²,

Peisker

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background:We studied ribosome and nucleoid distribution in Escherichia coli under growth and quiescence. Results: Spatially segregated ribosomes and nucleoids show drastically altered distribution in stationary phase or when treated with drugs affecting translation, transcription, nucleoid-topology, or cytoskeleton. Ribosome inheritance in daughter cells is frequently unequal. Conclusion: Cellular growth processes modulate ribosome and nucleoid distribution. Significance: This provides insight into subcellular organization of molecular machines.

show abstract

Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle

Cited by 79 publications

References 29 publications

In the Archaea Haloferax volcanii, Membrane Protein Biogenesis and Protein Synthesis Rates Are Affected by Decreased Ribosomal Binding to the Translocon

In the Archaea Haloferax volcanii, Membrane Protein Biogenesis and Protein Synthesis Rates Are Affected by Decreased Ribosomal Binding to the Translocon

Co-translational membrane association of the Escherichia coli SRP receptor

Organization of Ribosomes and Nucleoids in Escherichia coli Cells during Growth and in Quiescence

Contact Info

Product

Resources

About