PMID:24468661

Citation	Wang, P, Li, XZ, Cui, HR, Feng, YG and Wang, XY (2014) Identification and functional analysis of a novel parvulin-type peptidyl-prolyl isomerase from Gossypium hirsutum. Plant Physiol. Biochem. 76:58-66
Abstract	Plants have developed a variety of adaptive mechanisms to cope with stresses. A novel salt-induced gene was isolated during the screening of a NaCl-induced cDNA library of cotton seedlings. The gene was registered as accession number AY972810 in GenBank. Phylogenetic analysis suggested that the protein encoded by the gene belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases (PPIases, EC 5.2.1.8). Northern blot analysis indicated that the mRNA accumulation of GhPPI was induced by salt stress. Subcellular localization revealed that GhPPI (Gossypium hirsutum peptidyl-prolyl isomerase) was localized in the nucleus. The purified recombinant GhPPI could accelerate the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppressed protein aggregation under denaturing conditions using Gdn-HCl (guanidine hydrochloride), suggesting an additional chaperone activity. Several amino acid residues in GhPPI were speculated to be involved in substrate binding or catalysis based on molecular modeling and docking results. The activity of the peptidyl-prolyl isomerase was affected when the relevant amino acids were mutated. Among the 11 mutants, five amino acids mutations led to the enzyme activities decreased to 30% as that of wild type, and two reduced to approximately 60%. To the best of our knowledge, this is the first report of a plant parvulin PPIase involved in the salt stress response.
Links	PubMed Online version:10.1016/j.plaphy.2013.12.020
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
GOSHI:G8XQW2	enables	GO:0003755: peptidyl-prolyl cis-trans isomerase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
GOSHI:G8XQW2		GO:0003755: peptidyl-prolyl cis-trans isomerase activity	ECO:0000314:		F		Figure 4. Shows that the velocity of hydrolysis of the synthetic protein substrate is increased substantially in the presence of GhPPI in comparison to in its absence. This hydrolysis reaction demonstrates the protein’s PPIase activity.	complete CACAO 10108
YEAST:ESS1		GO:0030052: parvulin	ECO:0000314:		F		Accelerate the initial velocity of the cis-trans conversion of peptidly-prolyl bonds of a tetra peptide in a GhPPI concentration-dependent manner	complete CACAO 10586

References

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