ArticleGenome biology2002
The PRC-barrel: a widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism.
Article in Genome biology, 2002. 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, 61 citations in OpenAlex.
- CyanoTag: Discovery of protein function facilitated by high-throughput endogenous tagging in a photosynthetic prokaryote.Science advances · 2025Article
- Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division.Nature microbiology · 2024Article
- Widespread photosynthesis reaction centre barrel proteins are necessary for haloarchaeal cell division.Nature microbiology · 2024Article
- Article
- The two-component response regulator OrrA confers dehydration tolerance by regulating avaKa expression in the cyanobacterium Anabaena sp. strain PCC 7120.Environmental microbiology · 2022Article
- Characterization of Putative Sporulation and Germination Genes inMicroorganisms · 2022Article
- Protein Assistants of Small Ribosomal Subunit Biogenesis in Bacteria.Microorganisms · 2022Review
- Structural Basis for the C-Terminal Domain ofBiomolecules · 2021Article
- Global analysis of RNA-binding protein dynamics by comparative and enhanced RNA interactome capture.Nature protocols · 2021Article
- Evolutionary convergence and divergence in archaeal chromosomal proteins and Chromo-like domains from bacteria and eukaryotes.Scientific reports · 2018Article
- ESCRT-III mediated cell division in Sulfolobus acidocaldarius - a reconstitution perspective.Frontiers in microbiology · 2014Article
- Hypothetical proteins present during recovery phase of radiation resistant bacterium Deinococcus radiodurans are under purifying selection.Journal of molecular evolution · 2013Article
- Escherichia coli rimM and yjeQ null strains accumulate immature 30S subunits of similar structure and protein complement.RNA (New York, N.Y.) · 2013Article
- A genomic signature and the identification of new sporulation genes.Journal of bacteriology · 2013Article
- Gene conservation among endospore-forming bacteria reveals additional sporulation genes in Bacillus subtilis.Journal of bacteriology · 2013Article
- Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.Molecular cell · 2011Article
- Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB.PloS one · 2011Article
- Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.Biology direct · 2010Article
- Identification of a repressor of a truncated denitrification pathway in Moraxella catarrhalis.Journal of bacteriology · 2008Article
- Novel oxidative stress-responsive gene ERS25 functions as a regulator of the heat-shock and cell death response.The Journal of biological chemistry · 2008Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe H subunit of the purple bacterial photosynthetic reaction center (PRC-H) is important for the assembly of the photosynthetic reaction center and appears to regulate electron transfer during the reduction of the secondary quinone. It contains a distinct cytoplasmic beta-barrel domain whose fold has no close structural relationship to any other well known beta-barrel domain.
resultsWe show that the PRC-H beta-barrel domain is the prototype of a novel superfamily of protein domains, the PRC-barrels, approximately 80 residues long, which is widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain. Versions of this domain from photosynthetic proteobacteria contain a conserved acidic residue that is thought to regulate the reduction of quinones in the light-induced electron-transfer reaction. Closely related forms containing this acidic residue are also found in several non-photosynthetic bacteria, as well as in cyanobacteria, which have reaction centers with a different organization. We also show that the domain contains several determinants that could mediate specific protein-protein interactions.
conclusionsThe PRC-barrel is a widespread, ancient domain that appears to have been recruited to a variety of biological systems, ranging from RNA processing to photosynthesis. Identification of this versatile domain in numerous proteins could aid investigation of unexplored aspects of their biology.
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