PMID- 28461726
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20201001
IS  - 0971-5894 (Print)
IS  - 0974-0430 (Electronic)
IS  - 0974-0430 (Linking)
VI  - 23
IP  - 2
DP  - 2017 Apr
TI  - Insights into a key sulfite scavenger enzyme sulfite oxidase (SOX) gene in 
      plants.
PG  - 385-395
LID - 10.1007/s12298-017-0433-z [doi]
AB  - Sulfite oxidase (SOX) is a crucial molybdenum cofactor-containing enzyme in 
      plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation 
      pathway. However, studies of this crucial enzyme are quite limited hence this 
      work was attempted to understand the SOXs in four plant species namely, 
      Arabidopsis thaliana, Solanum lycopersicum, Populus trichocarpa and Brachypodium 
      distachyon. Herein studied SOX enzyme was characterized with both oxidoreductase 
      molybdopterin binding and Mo-co oxidoreductase dimerization domains. The 
      alignment and motif analyses revealed the highly conserved primary structure of 
      SOXs. The phylogeny constructed with additional species demonstrated a clear 
      divergence of monocots, dicots and lower plants. In addition, to further 
      understand the phylogenetic relationship and make a functional inference, a 
      structure-based phylogeny was constructed using normalized RMSD values in five 
      superposed models from four modelled plant SOXs herein and one previously 
      characterized chicken SOX structure. The plant and animal SOXs showed a clear 
      divergence and also implicated their functional divergences. Based on tree 
      topology, monocot B. distachyon appeared to be diverged from other dicots, 
      pointing out a possible monocot-dicot split. The expression patterns of sulfite 
      scavengers including SOX were differentially modulated under cold, heat, salt and 
      high light stresses. Particularly, they tend to be up-regulated under high light 
      and heat while being down-regulated under cold and salt stresses. The presence of 
      cis-regulatory motifs associated with different stresses in upstream regions of 
      SOX genes was thus justified. The protein-protein interaction network of AtSOX 
      and network enrichment with gene ontology (GO) terms showed that most predicted 
      proteins, including sulfite reductase, ATP sulfurylases and APS reductases were 
      among prime enzymes involved in sulfite pathway. Finally, SOX-sulfite docked 
      structures indicated that arginine residues particularly Arg374 is crucial for 
      SOX-sulfite binding and additional two other residues such as Arg51 and Arg103 
      may be important for SOX-sulfite bindings in plants.
FAU - Filiz, Ertugrul
AU  - Filiz E
AD  - Department of Crop and Animal Production, Cilimli Vocational School, Duzce 
      University, 81750 Cilimli, Duzce, Turkey. GRID: grid.412121.5
FAU - Vatansever, Recep
AU  - Vatansever R
AD  - Department of Biology, Faculty of Science and Arts, Marmara University, 34722 
      Goztepe, Istanbul, Turkey. GRID: grid.16477.33
FAU - Ozyigit, Ibrahim Ilker
AU  - Ozyigit II
AD  - Department of Biology, Faculty of Science and Arts, Marmara University, 34722 
      Goztepe, Istanbul, Turkey. GRID: grid.16477.33
LA  - eng
PT  - Journal Article
DEP - 20170322
PL  - India
TA  - Physiol Mol Biol Plants
JT  - Physiology and molecular biology of plants : an international journal of 
      functional plant biology
JID - 101304333
PMC - PMC5391365
OTO - NOTNLM
OT  - Docking
OT  - Macroelement
OT  - Modeling
OT  - PPI network
OT  - Stress
OT  - Sulfite
OT  - cis-Element
EDAT- 2017/05/04 06:00
MHDA- 2017/05/04 06:01
PMCR- 2018/04/01
CRDT- 2017/05/03 06:00
PHST- 2016/09/28 00:00 [received]
PHST- 2017/03/07 00:00 [revised]
PHST- 2017/03/16 00:00 [accepted]
PHST- 2017/05/03 06:00 [entrez]
PHST- 2017/05/04 06:00 [pubmed]
PHST- 2017/05/04 06:01 [medline]
PHST- 2018/04/01 00:00 [pmc-release]
AID - 433 [pii]
AID - 10.1007/s12298-017-0433-z [doi]
PST - ppublish
SO  - Physiol Mol Biol Plants. 2017 Apr;23(2):385-395. doi: 10.1007/s12298-017-0433-z. 
      Epub 2017 Mar 22.