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Abstract
Inositol polyphosphate 5-phosphatase (5PTase), a key enzyme that hydrolyzes the 5′ position of the inositol ring, has essential functions in growth, development, and stress responses in plants, yeasts, and animals. However, the evolutionary history and patterns of 5PTases have not been examined systematically. Here, we report a comprehensive molecular evolutionary analysis of the 5PTase gene family and define four groups. These four groups are different from former classifications, which were based on in vitro substrate specificity. Most orthologous groups appear to be conserved as single or low-copy genes in all lineages in Groups II–IV, whereas 5PTase genes in Group I underwent several duplication events in angiosperm, resulting in multiple gene copies. Whole-genome duplication (WGD) was the main mechanism for 5PTase duplications in angiosperm. Plant 5PTases have more members than that of animals, and most plant 5PTase genes appear to have evolved under strong purifying selection. The paralogs have diverged in substrate specificity and expression pattern, showing evidence of selection pressure. Meanwhile, the increase in 5PTases and divergences in sequence, expression, and substrate might have contributed to the divergent functions of 5PTase genes, allowing the angiosperms to successfully adapt to a great number of ecological niches.
Highlights
Phosphoinositides are phospholipids that are present ubiquitously in all eukaryotic cell membranes which regulate numerous cellular processes, including vesicular trafficking, cytoskeletal dynamics, proliferation, and survival [1,2,3,4]
Using the Hidden Markov model (HMM) algorithm, the complete set of 5PTases genes were identified from a comprehensive dataset that contained selected plants, animals, and fungi
Further investigation revealed that the copy number of the 5PTase genes varied considerably among plants, ranging from three in the green algae Chlamydomonas reinhardtii to 12 in Physcomitrella patens, 21 in Oryza sativa, and 15 in Arabidopsis thaliana, with the highest copy number being 39 in Glycine max
Summary
Phosphoinositides are phospholipids that are present ubiquitously in all eukaryotic cell membranes which regulate numerous cellular processes, including vesicular trafficking, cytoskeletal dynamics, proliferation, and survival [1,2,3,4]. The spatial and temporal localization of phosphoinositide signals is tightly regulated by phosphoinositide kinases and phosphatases, including the inositol polyphosphate. Pathway, are found in all kingdoms of life, and can dephosphorylate the second messenger molecules, inositol 1,4,5-trisphosphate (Ins(1,4,5)P3 ) and inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4 ) [2]. Previous studies have demonstrated the structure of the 5-phosphatase catalytic domain of Schizosaccharomyces pombe synaptojanin (SP synaptojanin), which is similar to those of. The catalytic mechanism of 5PTases remains unclear at present.
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