ArticleThe Journal of biological chemistry2013
Membrane association via an amino-terminal amphipathic helix is required for the cellular organization and function of RNase II.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- RNA exoribonucleases in E. coli.Archives of microbiology · 2026Review
- Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022Article
- Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021Review
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Membrane association of the bacterial riboregulator Hfq and functional perspectives.Scientific reports · 2017Article
- RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase.RNA (New York, N.Y.) · 2017Article
- Identification and Molecular Characterization of the Chloroplast Targeting Domain ofFrontiers in plant science · 2017Article
- MreBCD-associated Cytoskeleton is Required for Proper Segregation of the Chromosomal Terminus during the Division Cycle of Escherichia Coli.Chinese medical journal · 2015Article
- New insight into the structure and function of Hfq C-terminus.Bioscience reports · 2015Article
- The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome.Bioscience reports · 2014Article
- Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Molecular & cellular proteomics : MCP · 2014Article
- Initiation of mRNA decay in bacteria.Cellular and molecular life sciences : CMLS · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The subcellular localization of the exoribonuclease RNase II is not known despite the advanced biochemical characterization of the enzyme. Here we report that RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery and that RNase II is associated with the cytoplasmic membrane by its amino-terminal amphipathic helix. The helix also acts as an autonomous transplantable membrane binding domain capable of directing normally cytoplasmic proteins to the membrane. Assembly of the organized cellular structures of RNase II required the RNase II amphipathic membrane binding domain. Co-immunoprecipitation of the protein from cell extracts indicated that RNase II interacts with itself. The RNase II self-interaction and the ability of the protein to assemble into organized cellular structures required the membrane binding domain. The ability of RNase II to maintain cell viability in the absence of the exoribonuclease polynucleotide phosphorylase was markedly diminished when the RNase II cellular structures were lost due to changes in the amphipathicity of the amino-terminal helix, suggesting that membrane association and assembly of RNase II into organized cellular structures play an important role in the normal function of the protein within the bacterial cell.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.