Evidence map›Paper›PMID 17384167›Full record

ArticlePlant physiology2007

Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers.

Katsuhiro Nakayama, Kumiko Okawa, Tomohiro Kakizaki, Takenori Honma, Hideaki Itoh, Takehito Inaba

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. PsCor413pm2, a Plasma Membrane-Localized, Cold-Regulated Protein fromInternational journal of molecular sciences · 2018
    Article
  18. Article
  19. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Katsuhiro NakayamaThe 21st Century Centers of Excellence Program, Cryobiosystem Research Center, Iwate University, Morioka 020-8550, Japan.
Kumiko Okawa
Tomohiro Kakizaki
Takenori Honma
Hideaki Itoh
Takehito Inaba
Akita University · JPIwate University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many plants acquire increased freezing tolerance when they are exposed to nonfreezing temperatures of a certain duration. This process is known as cold acclimation and allows plants to protect themselves from freezing injury. A wide variety of polypeptides are induced during cold acclimation, among which is one encoded by COR15A in Arabidopsis (Arabidopsis thaliana). Previous studies showed that the COR15A gene encodes a small, plastid-targeted polypeptide that is processed to a mature form called Cor15am. In this study, we examined the biochemical properties and activities of Cor15am in more detail. We provide evidence that Cor15am localizes almost exclusively to the chloroplast stroma. In addition, the cold-regulated accumulation of Cor15am is affected by chloroplast functionality. Both gel-filtration chromatography and protein cross-linking reveal that Cor15am forms oligomers in the stroma of chloroplasts. Although Cor15am accumulates in response to low temperature, cold acclimation is not a prerequisite for oligomerization of Cor15am. Structural analysis suggests that Cor15am is composed of both ordered and random structures, and can stay soluble with small structural change after boiling and freeze-thaw treatments. Recombinant Cor15am exhibits in vitro cryoprotection of a freeze-labile enzyme, l-lactate dehydrogenase. Furthermore, Cor15am is capable of associating with l-lactate dehydrogenase in vitro and with potential stromal substrates in vivo. On the basis of these results, we propose that Arabidopsis Cor15am is a cryoprotective protein that forms oligomers in the chloroplast stroma, and that direct association of Cor15am with its substrates is part of its cryoprotective mechanism.

Indexed as

FreezingAcclimatizationArabidopsisArabidopsis ProteinsChloroplastsChromatography, GelL-Lactate DehydrogenaseMutationRecombinant Fusion ProteinsArabidopsis ProteinsCOR15 protein, ArabidopsisL-Lactate DehydrogenaseRecombinant Fusion Proteins

Identifiers

PMID17384167
PMCPMC1913801
OpenAlexW2103074638

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.