Evidence map›Paper›PMID 25699037›Full record

ArticleFrontiers in microbiology2015

Threonine 286 of fatty acid desaturase 7 is essential for ω-3 fatty acid desaturation in the green microalga Chlamydomonas reinhardtii.

Jong-Min Lim, Jayaraman Vikramathithan, Kwon Hwangbo, Joon-Woo Ahn, Youn-Il Park, Dong-Woog Choi, Won-Joong Jeong

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Increase in alpha-linolenic acid content by simultaneous expression of fatty acid metabolism genes in Sesame (Physiology and molecular biology of plants : an international journal of functional plant biology · 2022
    Article
  4. Review
  5. Article
  6. 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

7 authors at 4 institutions in 1 country.

Jong-Min LimSustainable Bioresource Center, Korea Institute of Bioscience and Biotechnology Daejeon, South Korea.
Jayaraman VikramathithanSustainable Bioresource Center, Korea Institute of Bioscience and Biotechnology Daejeon, South Korea.
Kwon HwangboSustainable Bioresource Center, Korea Institute of Bioscience and Biotechnology Daejeon, South Korea ; Department of Biological Science, Chungnam National University Daejeon, South Korea.
Joon-Woo AhnAdvanced Radiation Technology Institute - Korea Atomic Energy Research Institute Jeonbuk, South Korea.
Youn-Il ParkDepartment of Biological Science, Chungnam National University Daejeon, South Korea.
Dong-Woog ChoiDepartment of Biology Education, Chonnam National University South Korea.
Won-Joong JeongSustainable Bioresource Center, Korea Institute of Bioscience and Biotechnology Daejeon, South Korea.
Korea Research Institute of Bioscience and Biotechnology · KRChungnam National University · KRChonnam National University · KRKorea Atomic Energy Research Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Omega-3 fatty acid desaturases catalyze the conversion of dienoic fatty acids (C18:2 and C16:2) into trienoic fatty acids (C18:3 and C16:3), accounting for more than 50% of the total fatty acids in higher plants and the green microalga Chlamydomonas reinhardtii. Here, we describe a Thr residue located in the fourth transmembrane domain of fatty acid desaturase 7 (FAD7) that is essential for the biosynthesis of ω-3 fatty acids in C. reinhardtii. The ω-3 fatty acid deficiency in strain CC-620, which contains a putative missense mutation at Thr286 of CrFAD7, was recovered by the overexpression of CC-125 CrFAD7. A Ser substitution in position 286 was able to partially complement the phenotype of the ω-3 fatty acid deficiency, but other substitution variants, such as Tyr, His, Cys, and Gly, failed to do so. Prediction of the phosphorylation target site revealed that Thr286 may be phosphorylated. Analysis of the structural conformation of CC-620 CrFAD7 via topology prediction (and bends in the helix) shows that this missense mutation may collapse the catalytic structure of CrFAD7. Taken together, this study suggests that Thr286 is essential for the maintaining the catalytic structure of CrFAD7.

Indexed as

Chlamydomonas reinhardtiiCrFAD7fatty acid desaturaseThr286topology

Identifiers

PMID25699037
PMCPMC4318421
OpenAlexW2066101432

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.