Evolutionary and Structural Analysis of PP16 in Viridiplantae

• Published in: International journal of molecular sciences 2024-02, Vol.25 (5), p.2839
• Main Authors: Jiménez-López, Domingo, Xoconostle-Cázares, Beatriz, Calderón-Pérez, Berenice, Vargas-Hernández, Brenda Yazmín, Núñez-Muñoz, Leandro Alberto, Ramírez-Pool, José Abrahán, Ruiz-Medrano, Roberto
• Format: Article
• Language: English
• Subjects: Algae; Biological Transport; Citrus fruits; Flowers & plants; Genomes; NMR; non-cell autonomous protein; Nuclear magnetic resonance; Peptides; Phloem - metabolism; phloem protein 16; phloem transport; Phylogenetics; phylogeny; Plant genetics; Plant Proteins - genetics; Plants - metabolism; Protein binding; Proteins; RNA; Viridiplantae - metabolism
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms25052839

Members of the phloem protein 16 (PP16) gene family are induced by elicitors in rice and the corresponding proteins from cucurbits, which display RNA binding and intercellular transport activities, are accumulated in phloem sap. These proteins facilitate the movement of protein complexes through the phloem translocation flow and may be involved in the response to water deficit, among other functions. However, there is scant information regarding their function in other plants, including the identification of paralog genes in non-vascular plants and chlorophytes. In the present work, an evolutionary and structural analysis of the PP16 family in green plants (Viridiplantae) was carried out. Data mining in different databases indicated that likely originated from a larger gene present in an ancestral lineage that gave rise to chlorophytes and multicellular plants. This gene encodes a protein related to synaptotagmin, which is involved in vesicular transport in animal systems, although other members of this family play a role in lipid turnover in endomembranes and organelles. These proteins contain a membrane-binding C2 domain shared with PP16 proteins in vascular plants. In silico analysis of the predicted structure of the PP16 protein family identified several β-sheets, one α-helix, and intrinsically disordered regions. PP16 may have been originally involved in vesicular trafficking and/or membrane maintenance but specialized in long-distance signaling during the emergence of the plant vascular system.