Evidence map›Paper›PMID 25100720›Full record

ArticleThe Journal of biological chemistry2014

Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase.

Rebecca L Roston, Kun Wang, Leslie A Kuhn, Christoph Benning

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Rebecca L RostonDepartments of Biochemistry and Molecular Biology and Michigan State University, East Lansing, Michigan 48824. Electronic address: rroston@unl.edu.
Kun WangDepartments of Biochemistry and Molecular Biology and Michigan State University, East Lansing, Michigan 48824.
Leslie A KuhnDepartments of Biochemistry and Molecular Biology and Michigan State University, East Lansing, Michigan 48824; Departments of Computer Science and Engineering, Michigan State University, East Lansing, Michigan 48824.
Christoph BenningDepartments of Biochemistry and Molecular Biology and Michigan State University, East Lansing, Michigan 48824.
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SENSITIVE TO FREEZING 2 (SFR2) is classified as a family I glycosyl hydrolase but has recently been shown to have galactosyltransferase activity in Arabidopsis thaliana. Natural occurrences of apparent glycosyl hydrolases acting as transferases are interesting from a biocatalysis standpoint, and knowledge about the interconversion can assist in engineering SFR2 in crop plants to resist freezing. To understand how SFR2 evolved into a transferase, the relationship between its structure and function are investigated by activity assay, molecular modeling, and site-directed mutagenesis. SFR2 has no detectable hydrolase activity, although its catalytic site is highly conserved with that of family 1 glycosyl hydrolases. Three regions disparate from glycosyl hydrolases are identified as required for transferase activity as follows: a loop insertion, the C-terminal peptide, and a hydrophobic patch adjacent to the catalytic site. Rationales for the effects of these regions on the SFR2 mechanism are discussed.

Indexed as

Amino Acid MotifsAmino Acid SequenceArabidopsisArabidopsis Proteinsbeta-GlucosidaseCatalytic DomainConserved SequenceHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsModels, MolecularMolecular Sequence DataProtein BindingSequence Homology, Amino AcidStructural Homology, ProteinArabidopsis Proteinsbeta-GlucosidaseIntrinsically Disordered ProteinsSFR2 protein, ArabidopsisChloroplastFreezingGlycosidaseGlycosyl HydrolaseGlycosyltransferaseHydrolaseMembrane TurnoverOligogalactolipidStress ResponseTransferase

Identifiers

PMID25100720
PMCPMC4176223
OpenAlexW2135396734

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.