ArticleNucleic acids research2009
SrmB, a DEAD-box helicase involved in Escherichia coli ribosome assembly, is specifically targeted to 23S rRNA in vivo.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 56 citations in OpenAlex.
- Article
- DEAD Box RNA Helicases: Biochemical Properties, Role in RNA Processing and Ribosome Biogenesis.Cell biochemistry and biophysics · 2024Review
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- Near-physiological in vitro assembly of 50S ribosomes involves parallel pathways.Nucleic acids research · 2023Article
- Long-term ecological and evolutionary dynamics in the gut microbiomes of carbapenemase-producing Enterobacteriaceae colonized subjects.Nature microbiology · 2022Article
- Study of key RNA metabolism proteins inRNA biology · 2020Article
- SrmB Rescues Trapped Ribosome Assembly Intermediates.Journal of molecular biology · 2020Article
- A DEAD-box protein regulates ribosome assembly through control of ribosomal protein synthesis.Nucleic acids research · 2019Article
- The impact of recent improvements in cryo-electron microscopy technology on the understanding of bacterial ribosome assembly.Nucleic acids research · 2017Review
- Fluorescence bimolecular complementation enables facile detection of ribosome assembly defects in Escherichia coli.RNA biology · 2016Article
- The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation.Nucleic acids research · 2016Article
- Single methylation of 23S rRNA triggers late steps of 50S ribosomal subunit assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The DEAD-box helicase Ded1 from yeast is an mRNP cap-associated protein that shuttles between the cytoplasm and nucleus.Nucleic acids research · 2014Article
- RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014Review
- Potential regulatory interactions of Escherichia coli RraA protein with DEAD-box helicases.The Journal of biological chemistry · 2013Article
- DExD/H-box RNA helicases in ribosome biogenesis.RNA biology · 2013Review
- RNA helicases: diverse roles in prokaryotic response to abiotic stress.RNA biology · 2013Review
- Recognition of the 70S ribosome and polysome by the RNA degradosome in Escherichia coli.Nucleic acids research · 2012Article
- A Listeria monocytogenes RNA helicase essential for growth and ribosomal maturation at low temperatures uses its C terminus for appropriate interaction with the ribosome.Journal of bacteriology · 2012Article
- How much can we learn about the function of bacterial rRNA modification by mining large-scale experimental datasets?Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEAD-box proteins play specific roles in remodeling RNA or ribonucleoprotein complexes. Yet, in vitro, they generally behave as nonspecific RNA-dependent ATPases, raising the question of what determines their specificity in vivo. SrmB, one of the five Escherichia coli DEAD-box proteins, participates in the assembly of the large ribosomal subunit. Moreover, when overexpressed, it compensates for a mutation in L24, the ribosomal protein (r-protein) thought to initiate assembly. Here, using the tandem affinity purification (TAP) procedure, we show that SrmB forms a complex with r-proteins L4, L24 and a region near the 5'-end of 23S rRNA that binds these proteins. In vitro reconstitution experiments show that the stability of this complex reflects cooperative interactions of SrmB with L4, L24 and rRNA. These observations are consistent with an early role of SrmB in assembly and explain the genetic link between SrmB and L24. Besides its catalytic core, SrmB possesses a nonconserved C-terminal extension that, we show, is not essential for SrmB function and specificity. In this regard, SrmB differs from DbpA, another DEAD-box protein involved in ribosome assembly.
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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.