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rnlA RNase LS, toxin of the RnlAB toxin-antitoxin system [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947107, updated on 3-Dec-2024

Summary

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Official Symbol
rnlA
Official Full Name
RNase LS, toxin of the RnlAB toxin-antitoxin system
Primary source
ECOCYC:G7365
Locus tag
b2630
See related
ASAP:ABE-0008659
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2626; std; yfjN
Summary
RnlA is responsible for the rapid degradation of T4 late genes in T4 dmd mutants. [More information is available at EcoGene: EG13200]. RNase LS is an endoribonuclease that cleaves bacteriophage T4 late mRNA in dmd mutant strains . [More information is available at EcoCyc: G7365].
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Genomic context

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Sequence:
NC_000913.3 (2765918..2766991)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative helicase YfjK Neighboring gene anti-bacteriophage protein Neighboring gene protein YfjM Neighboring gene antitoxin RnlB Neighboring gene putative GTP-binding protein YfjP Neighboring gene DUF932 domain-containing protein YfjQ

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance. Wei Y, et al. Mol Microbiol, 2013 Dec. PMID 24112600
  2. A novel endoribonuclease, RNase LS, in Escherichia coli. Otsuka Y, et al. Genetics, 2005 Jan. PMID 15677746, Free PMC Article
  3. RNA cleavage linked with ribosomal action. Yamanishi H, et al. Genetics, 2005 Oct. PMID 16020788, Free PMC Article
  4. Opposite roles of the dmd gene in the control of RNase E and RNase LS activities. Kanesaki T, et al. Genes Genet Syst, 2005 Aug. PMID 16284417
  5. Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA. Garcia-Rodriguez G, et al. Nucleic Acids Res, 2021 Jul 9. PMID 34139012, Free PMC Article

See all (21) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA.
    Title: Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA.
  2. RNase HI recruits RnlB to RnlA through N-repeated domain for inhibiting RnlA toxicity and thus plays two contrary roles in the regulation of RnlA-RnlB system.
    Title: RnlB Antitoxin of the Escherichia coli RnlA-RnlB Toxin-Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity.
  3. Here, authors provide the evidence that RNase HI is an essential factor for activation of RnlA.
    Title: RNase HI stimulates the activity of RnlA toxin in Escherichia coli.
  4. Results suggest that RnlA functions as a toxin with mRNA endoribonuclease activity and is inhibited after binding to T4 antitoxin Dmd protein through its Dmd-binding domain.
    Title: Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance.
  5. RNase LS regulates Crp-cAMP concentration by degrading the cyaA transcripts.
    Title: Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia coli.
  6. Fractionation of the RNase LS activity in a cell extract showed that it sedimented through a sucrose density gradient as a 1000-kDa complex that included RnlA. Pull-down experiments revealed more than 10 proteins associated with His-tagged RnlA.
    Title: A role of RnlA in the RNase LS activity from Escherichia coli.
  7. RNase LS cleaves soc RNA in a manner dependent on translation termination.
    Title: RNA cleavage linked with ribosomal action.
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General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables RNA endonuclease activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA endonuclease activity IEA
Inferred from Electronic Annotation
more info
  
enables endonuclease activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in defense response to virus IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within mRNA catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of DNA-templated transcription NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in regulation of growth NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in single-species biofilm formation NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
part_of toxin-antitoxin complex IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

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Preferred Names
RNase LS, toxin of the RnlAB toxin-antitoxin system

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    2765918..2766991
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417119.1 RNase LS, toxin of the RnlAB toxin-antitoxin system [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417119.1

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    P52129
    Conserved Domains (3) summary
    cd14794
    Location:7 → 97
    RNLA_N_1; N-terminal repeat domain of toxin RnlA; first out of two repeats
    cd14795
    Location:99 → 184
    RNLA_N_2; N-terminal repeat domain of toxin RnlA; second out of two repeats
    pfam19034
    Location:203 → 325
    RnlA-toxin_C; RNase LS, bacterial toxin C terminal
Nucleotide Protein
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