Abstract
Juvenile hormone (JH) plays a critical role in many physiological activities of Arthropoda. Juvenile hormone acid methyltransferase (JHAMT) is involved in the last steps of JH biosynthesis as an important rate-limiting enzyme. In recent studies, an increasing number of JHAMTs were identified in arthropods, but no JHAMT was reported in spiders. Herein, eight JHAMTs were identified in the pond wolf spider, Pardosa pseudoannulata, all containing the well conserved S-adenosyl-L-methionine binding motif. JHAMT-1 and the other seven JHAMTs were located at chromosome 13 and chromosome 1, respectively. Multiple alignment and phylogenetic analysis showed that JHAMT-1 was grouped together with insect JHAMTs independently and shared high similarities with insect JHAMTs compared to the other seven JHAMTs. In addition, JHAMT-1, JHAMT-2, and JHAMT-3 were highly expressed in the abdomen of spiderlings and could respond to the stimulation of exogenous farnesoic acid. Meanwhile, knockdown of these three JHAMTs caused the overweight and accelerated molting of spiderlings. These results demonstrated the cooperation of multi-JHAMTs in spider development and provided a new evolutionary perspective of the expansion of JHAMT in Arachnida.
Highlights
Juvenile hormone acid methyltransferase (JHAMT) catalyzes the methylation in the last steps of juvenile hormone III (JH III) biosynthesis, converting farnesoic acid (FA) to methyl farnesoate (MF) or converting Juvenile hormone (JH) III acid (JHA III) to JH III [1,7]
Full-length JHAMTs were identified in P. pseudoannulata, namely, JHAMT-1, -2, 2
MZ321025, MZ321026, MZ321027, MZ321028, MZ321029, MZ321030, and MZ321031, Eight full-length JHAMTs were identified in P. pseudoannulata, namely, JHAMT-1, -2, -3, respectively)
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Juvenile hormone acid methyltransferase (JHAMT) is a highly specific rate-limiting enzyme in JH biosynthesis in insects [7]. It belongs to the family of S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTs) which transfer a methyl group from methyl donor SAM to the carboxyl group of substrates [7,8]. We took advantage related to the identification and function of JHAMT in JH biosynthesis was reported in spiders. We took advantage of the genomic and transcriptomic databases to identify and characterize JHAMTs in the pond wolf spider Pardosa pseudoannulata. The function of JHAMTs in spider development was demonstrated by RNA interference (RNAi).
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