ArticleBMC evolutionary biology2013
The unique evolution of the programmed cell death 4 protein in plants.
Article in BMC evolutionary biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Cell death in bryophytes: emerging models to study core regulatory modules and conserved pathways.Annals of botany · 2024Review
- Analysis of domain organization and functional signatures of trypanosomatid keIF4Gs.Molecular and cellular biochemistry · 2022Article
- Responses of Marine Diatom Skeletonema marinoi to Nutrient Deficiency: Programmed Cell Death.Applied and environmental microbiology · 2020Article
- Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions.International journal of molecular sciences · 2019Review
- Identification and Analysis of OVATE Family Members from Genome of the Early Land Plants Provide Insights into Evolutionary History of OFP Family and Function.Journal of molecular evolution · 2018Article
- Evolution and palaeophysiology of the vascular system and other means of long-distance transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Article
- Roles of plant hormones and anti-apoptosis genes during drought stress in rice (Oryza sativa L.).3 Biotech · 2016Article
- Unfoldome variation upon plant-pathogen interactions: strawberry infection by Colletotrichum acutatum.Plant molecular biology · 2015Article
- Comparative transcriptome analysis to reveal genes involved in wheat hybrid necrosis.International journal of molecular sciences · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe programmed cell death 4 (PDCD4) protein is induced in animals during apoptosis and functions to inhibit translation and tumor promoter-induced neoplastic transformation. PDCD4 is composed of two MA3 domains that share similarity with the single MA3 domain present in the eukaryotic translation initiation factor (eIF) 4G, which serves as a scaffold protein to assemble several initiation factors needed for the recruitment of the 40S ribosomal subunit to an mRNA. Although eIF4A is an ATP-dependent RNA helicase that binds the MA3 domain of eIF4G to promote translation initiation, binding of eIF4A to the MA3 domains of PDCD4 inhibits protein synthesis. Genes encoding PDCD4 are present in many lower eukaryotes and in plants, but PDCD4 in higher plants is unique in that it contains four MA3 domains and has been implicated in ethylene signaling and abiotic stress responses. Here, we examine the evolution of PDCD4 in plants.
resultsIn older algal lineages, PDCD4 contains two MA3 domains similar to the homolog in animals. By the appearance of early land plants, however, PDCD4 is composed of four MA3 domains which likely is the result of a duplication of the two MA3 domain form of the protein. Evidence from fresh water algae, from which land plants evolved, suggests that the duplication event occurred prior to the colonization of land. PDCD4 in more recently evolved chlorophytes also contains four MA3 domains but this may have resulted from an independent duplication event. Expansion and divergence of the PDCD4 gene family occurred during land plant evolution with the appearance of a distinct gene member following the evolution of basal angiosperms.
conclusionsThe appearance of a unique form of PDCD4 in plants correlates with the appearance of components of the ethylene signaling pathway, suggesting that it may represent the adaptation of an existing protein involved in programmed cell death to one that functions in abiotic stress responses through hormone signaling.
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