Cited by 22Plant Molecular Biology ResearchCell death mechanisms and regulationChromosomal and Genetic Variations

The unique evolution of the programmed cell death 4 protein in plants

Open access
Cheng, Shijun, Liu, Renyi, Gallie, Daniel R·2013·BMC Evolutionary Biology

Abstract

Background: The 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. Results: In 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. Conclusions: The 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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1186/1471-2148-13-199

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The PDCD4 gene homolog is present in plants but not in yeasts.

    “The gene homolog is present in plants but not in yeasts [16].”

    From Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions (2019) · cites this paper as [16]

    The Background states that PDCD4 homologs are present in plants, but says only that none has been reported in yeast. The claim turns that qualified observation into a categorical assertion that the homolog is absent from yeasts. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • The PDCD4 gene is well conserved in species; human and fish (elephant shark) protein sequences are 72% identical.

    “The gene is well conserved in species; for example, the homology between human and fish (elephant shark) is 72 % identical in the protein level.”

    From Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions (2019) · cites this paper as [16]

    The Results section ('The four MA3 domain PDCD4 protein is unique to plants'; page unavailable) reports considerable conservation among angiosperm PDCD4 proteins and identifies homologs in animals. It does not report a human–elephant shark comparison or 72% protein-sequence identity (searched: 'elephant shark' and '72%'). (LLM, conf=0.85)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Cheng, S., Liu, R., & Gallie, D. R.
Affiliations
University of California, Riverside (US)
Corresponding author
Gallie, Daniel R
Venue
BMC Evolutionary Biology
Published
2013-09-16
Volume
13
Issue
1
Pages
199-199
ISSN
1471-2148 (ISSN-L)
OpenAlex
W2069441791
Cited by
22
References
43
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2022: 1 · 2020: 3 · 2019: 5 · 2018: 1 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 2
FWCI
2.01
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • BMC Evolutionary Biology (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • National Science Foundation (0820047)
  • Division of Agriculture and Natural Resources, University of California
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Chromosomal and Genetic Variations
Keywords
PDCD4, eIF4G, eIF4A, translation initiation, gene duplication, land plant evolution, Chlorophyta, ethylene signaling, abiotic stress response, gene family evolution, protein evolution
MeSH terms
Amino Acid Sequence, Chlamydomonas, Molecular Sequence Data, Plant Proteins, Plants, RNA, Messenger, Protein Biosynthesis, Signal Transduction, Sequence Alignment, Apoptosis, Protein Structure, Tertiary, Evolution, Molecular, Eukaryotic Initiation Factor-4F, Apoptosis Regulatory Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review