Polyamines interaction with thylakoid proteins during stress.

The involvement of polyamines in plant responses to abiotic stresses is well investigated, while there has been few reports on the specific mode of action of polyamines on the photosynthetic apparatus. The objective of this review is thus to examine the mode of interaction of polyamines with proteins of photosystem II core and LHCII, including methylamine (monoamine) as a simplified model to better understand the mode of action of polyamines. Spectroscopic methods used to determine the binding mode of amines with PSII proteins showed that amines such as spermine, putrescine and methylamine interact with protein (H-bonding) through polypeptide C=O, C-N and N-H groups with major perturbations of protein secondary structure as the concentration of amines was raised. High concentration of amines added to PSII-enriched submembrane fractions causes a significant loss of PSII activity. However, at lower concentration, polyamines, especially spermine, improve the photosynthetic functions under stress. We concluded from this review that besides the conjugation of polyamines with LHC polypeptides, polyamines are likely to interact with extrinsic proteins and the hydrophilic part of intrinsic proteins of PSII by electrostatic interaction. This could stabilize the conformation of proteins under various stresses. However, at high concentration of polyamines a strong inhibition of PSII activity is observed.