Salt-affected soil is a prominent challenge in agriculture. Nowadays, more than 800 million hectares of land (about 6% of the world’s total land area) are induced with high salt concentrations, and thus, are unsuitable for growing typically salt-sensitive crop plants. The ongoing salinization of arable land exacerbates this limitation. To address this issue, the development of salinity-tolerant crop plants has gained considerable interest, with a protein identified by Prof. Mark Tester's group, named "SALTY2," offering promising potential. SALTY2 is overexpressed in response to NaCl treatment on Salicornia plants conferring salinity tolerance, and following the function of the SALTY2 protein from Salicornia and analogous proteins in Arabidopsis, yeast and in vitro, a universal mechanism in evolution is suggested. During my thesis, we analyzed the biophysical properties of SALTY2, and based on spectroscopic methods we confirmed it is an intrinsic disordered protein (IDP), which is consistent with previous studies claiming that IDPs play a vital role in stress response pathways. We have identified and characterized the loss-of-function "RG/RGG" to "KG/KGG" type mutation and a deltaSTM1 N-terminal mutation, and investigated the interaction of SALTY2 and other cellular components, including short fragment RNA, and 80S ribosome. Together with state-of-the-art high-resolution NMR and Cryo-EM methods we validated the direct interaction of SALTY2 with plant ribosomes, and 25nts random RNA, and determined the 3D structure of ribosome with the potential binding site of the SALTY2 protein. Combining biophysical, structural and functional analyses of the wild-type and loss-of-function mutants of SALTY2, we proposed a potential mechanism by which the IDP protein SALTY2 confers salinity tolerance in plants. These findings offer a deeper understanding of the molecular basis of salinity tolerance in plants via IDPs and contribute to the ongoing efforts to develop salinity-tolerant crop plants.