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Molecular Properties of Disordered Plant Dehydrins- Membrane Interaction and Function in Stress

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Molecular Properties of Disordered Plant Dehydrins- Membrane Interaction and Function in Stress Molecular properties of disordered plant dehydrins- Membrane interaction and function in stress Sylvia Eriksson Molecular properties of disordered plant dehydrins Membrane interaction and function in stress Sylvia Eriksson Abstract Dehydrins are intrinsically disordered plant stress-proteins. Repetitively in their sequence are some highly conserved stretches of 7-17 residues, the so called K-, S-, Y- and lysine rich segments. This thesis aims to give insight into the possible role dehydrins have in the stressed plant cell with main focus on membrane interaction and protection. The work includes four re- combinant dehydrins from the plant Arabidopsis thaliana: Cor47 (SK3), Lti29 (SK3), Lti30 (K6) and Rab18 (Y2SK2). Initially, we mimicked crowded cellular environment in vitro to verify that dehydrins are truly disordered proteins. Thereafter, the proposal that the compulsory K-segment determines membrane binding was tested. Experi- ments show that only Lti30 and Rab18 bind, whereas Cor47 and Lti29 does not. As Lti30 and Rab18 binds they assembles vesicles into clusters in vitro, a feature used to characterize the interaction. From this it was shown that membrane binding of Lti30 is electrostatic and determined by global as well as local charges. Protonation of histidine pairs flanking the K-segments works as an on/off-binding switch. By NMR studies it was shown that the K- segments form a dynamic α-helix upon binding, so called disorder-to-order behaviour. Also, dehydrins electrostatic interaction with lipids can be further tuned by posttranslational phosphorylation or coordination of calcium and zinc ions. Finally, specific binding of Rab18 to inositol lipids, mainly PI(4,5)P2, is reported. The interaction is mainly coordinated by two arginines neighboring one of the K-segments. In conclusion, the K-segments are indeed involved in the binding of dehydrins to membrane but only in combination with exten- sions (Lti30) or modified (Rab18). Keywords: abiotic stress; dehydrin; intrinsically disordered proteins; Lea- proteins; phospholipids Publications This thesis is based on following papers, which will be referred to by their roman numerals. Paper I Mouillon J. M., Eriksson S. K. and Harryson P. Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehy- drin proteins are highly resistant to structural collapse. Plant Physiol. 2008, 148(4): 1925-1937. Paper II Eriksson S. K. *, Kutzer M. *, Procek J., Gröbner G. and Harryson P. Tuna- ble membrane binding of the intrinsically disordered dehydrin Lti30, a cold- induced plant stress protein. Plant Cell 2011, 23(6): 2391-2404. Paper III Eriksson S.K., Eremina N., Barth A., Danielsson J. and Harryson P. Mem- brane-induced folding of the plant stress dehydrin Lti30. Plant Physiol. 2016, 171(2): 932-943. Paper IV Eriksson S.K., Danielsson J and Harryson P. Membrane binding of disor- dered plant dehydrins is tuned by phosphorylation and coordination of Ca2+ and Zn2+ ions. Manuscript Paper V Eriksson S.K. and Harryson P. Rab18 dehydrin –a stressed induced condi- tional peripheral membrane protein. Specific interaction with PI(4,5)P2 Manuscript * These authors contributed equally Paper I, II and III are Copyright by the American Society of Plant Biologists. 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"((4DDDDDDDDDDDDDDDDDDDDDDDDSS !"# #"" ! $ #!" Abbreviations Lea Late Embryogenesis Abundant PC Phosphatidylcholine PG Phosphatidylglycerol PS Phosphatidylserine PA Phosphatidic acid PI Phosphatidylinositol PIP Phosphatidylinositol phosphate PIP2 Phosphatidylinositol bisphosphate LUV Large Unilamellar Vesicles ABA Abscisic acid CD Circular Dichroism NMR Nuclear Magnetic Resonance FTIR Fourier Transform Infrared Spectroscopy Amino acids A Ala Alanine C Cys Cysteine D Asp Aspartate E Glu Glutamate F Phe Phenylalanine G Gly Glycine H His Histidine I Ile Isoleucine K Lys Lysine L Leu Leucine M Met Methionine N Asn Asparagine P Pro Proline Q Gln Glutamine R Arg Arginine S Ser Serine T Thr Threonine V Val Valine W Trp Tryptophan Y Tyr Tyrosine 1. Introduction During recent years the world has been exposed to abnormal weather fluctu- ations causing drought fields and a severe damage of food production. Ex- tended periods of drought have occurred mainly in Africa, North America, China, Australia and Brazil. As the same time as arable crops are reduced, the world’s population and demand for food are increasing. Plants are on a regularly basis naturally exposed to cycles in temperature, soil salinity and drought. When these conditions become stressful to the plant, it is called abiotic stress, which may affect both plant growth and crop production. This thesis elucidates the function of a group of plant stress pro- teins, the dehydrins, studied at a molecular level in an attempt to reveal their role in plant stress survival. The outer border of a cell consists of a cell membrane that distinguishes it from its surroundings. Inside are a wide variety of proteins that perform different cellular reactions such as enzymes and proteins, which control gene expression. Alterations in temperature, water and salinity lead to a reduction in cellular water content to which the cell is sensitive. Even small changes in water levels affect the performance of both cell membranes and proteins. When conditions are changing fast and growth conditions are poor, the plant is considered to be under stress. If the stress persists the plant may finally die. However, desiccation can also be a natural condition such as in pollen or seeds (Ingram and Bartels 1996). Most plants are rooted to the ground and cannot move when they are ex- posed to stress; they have to stay and adopt. They have therefor developed several protection mechanisms to maintain cellular functions. This response system includes: inductions of different stress proteins like the dehydrins and chaperones and molecules that maintain cell turgor (sugars, betaine, proline) (Ingram and Bartels 1996). Expression of the plant specific dehydrins is induced during different water stresses. Dehydrins are intrinsically disordered proteins and lack a fixed 3D structure. The precise in vivo function of dehydrins is still unclear, but under periods of stress, most plant produce high amounts of dehydrins, which must reflect an important role in plant survival. This proposal is experimentally 11 confirmed, since plants overexpressing dehydrins have been shown to have a higher survival rate when stressed compared to wild plant types (Houde et al., 2004; Puhakainen et al., 2004; Brini et al., 2007). The focus of this thesis lies within the discussion of the molecular functions of the dehydrins, in particular membrane binding. The following chapters include a short introduction to plant stress and stress defense. Finally, the results are discussed with
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