ReviewProtein science : a publication of the Protein Society2020
PhoH2 proteins couple RNA helicase and RNAse activities.
Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Structural insights into higher-order natural RNA-only multimers.Nature structural & molecular biology · 2025Article
- Unveiling the probiotic potential of the genus Geobacillus through comparative genomics and in silico analysis.Scientific reports · 2025Article
- RNA-binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria.Nature communications · 2025Article
- A conservedMicrobiology (Reading, England) · 2025Article
- Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024Article
- TheJournal of bacteriology · 2023Article
- ThebioRxiv : the preprint server for biology · 2023Article
- Comparative Analysis on Proteomics Profiles of Intracellular and ExtracellularFrontiers in genetics · 2022Article
- Jumbo Phages: A Comparative Genomic Overview of Core Functions and Adaptions for Biological Conflicts.Viruses · 2021Article
- PhoH2 proteins couple RNA helicase and RNAse activities.Protein science : a publication of the Protein Society · 2020Review
- Post-transcriptional modulation of the SigF regulon in Mycobacterium smegmatis by the PhoH2 toxin-antitoxin.PloS one · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PhoH2 proteins are found in a very diverse range of microorganisms that span bacteria and archaea. These proteins are composed of two domains: an N-terminal PIN-domain fused with a C-terminal PhoH domain. Collectively this fusion functions as an RNA helicase and ribonuclease. In other genomic contexts, PINdomains and PhoHdomains are separate but adjacent suggesting association to achieve similar function. Exclusively among the mycobacteria, PhoH2 proteins are encoded in the genome with an upstream gene, phoAT, which is thought to play the role of an antitoxin (in place of the traditional VapB antitoxin that lies upstream of the 47 other PINdomains in the mycobacterial genome). This review examines PhoH2 proteins as a whole and describes the bioinformatics, biochemical, structural, and biological properties of the two domains that make up PhoH2: PIN and PhoH. We review the transcriptional regulators of phoH2 from two mycobacterial species and speculate on the function of PhoH2 proteins in the context of a Type II toxin-antitoxin system which are thought to play a role in the stress response in bacteria.
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Registered trials
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.