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Changes in Water Availability or Molecular Crowding Induce Folding in Instrinsically Disordered Stress Proteins from Plants
Author(s) -
Covarrubias Alejandra,
CuevasVelazquez César,
RiveraNajera Lucero,
RendonLuna David,
SaabRincón Gloria,
MartinezYamout Maria,
Dyson H Jane,
Amero Carlos
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.712.11
Subject(s) - folding (dsp implementation) , protein folding , intrinsically disordered proteins , chemistry , biophysics , protein secondary structure , water stress , function (biology) , microbiology and biotechnology , in vitro , protein structure , biochemistry , biology , botany , electrical engineering , engineering
Late Embryogenesis Abundant (LEA) proteins are a broadly distributed group involved in the plant response to water deficit. Most of them are predicted to be intrinsically disordered. By partial dehydration and freeze‐thaw in vitro assays, it was shown that some LEA proteins protect other proteins from the effects of water deficit. Given the presumed unstructured character of LEA proteins, we hypothesized that their flexible nature plays a critical role in their interaction with diverse partners. This structural flexibility might be modulated by the cell water status, promoting conformations needed to interact with specific targets. In this work, we report some of the structural and functional properties of LEA proteins from groups 4 and 6. We showed that proteins in both groups are intrinsically unstructured in solution; however, their intrinsic potential to form secondary structure was exhibited by treatment with a structure inducer, which promoted a significant α‐helix formation. A decrease in water availability and an increase in molecular crowding induced folding in both LEA protein groups but in different level. We also determined the protection efficiency of group 4 LEA proteins and proposed a mechanism for this function. This work was partially supported by CONACyT (132258) and DGAPA‐UNAM (IN208212).