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Farnesoic acid O‐methyl transferase (FAMeT) isoforms: Conserved traits and gene expression patterns related to caste differentiation in the stingless bee, Melipona scutellaris
Author(s) -
Vieira Carlos U.,
Bonetti Ana M.,
Simões Zilá L.P.,
Maranhão Andréa Q.,
Costa Christiane S.,
Costa Maria Cristina R.,
Siquieroli Ana Carolina S.,
Nunes Francis M.F.
Publication year - 2008
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20224
Subject(s) - biology , gene isoform , juvenile hormone , gene , alternative splicing , genetics , transferase , gene expression , in silico , biochemistry , enzyme , hormone
Abstract Farnesoic acid O‐methyl transferase (FAMeT) is the enzyme that catalyzes the formation of methyl farnesoate (MF) from farnesoic acid (FA) in the biosynthetic pathway of juvenile hormone (JH). This work reports the cloning, sequencing, and expression of FAMeT gene from the stingless bee Melipona scutellaris (MsFAMeT). The MsFAMeT in silico analysis showed that greatest sequence similarity is found in Apis mellifera and other insects, while relatively less similarity is shown in crustaceans. Evidence of alternative splicing of a 27 nucleotide (nt) microexon explains the presence of the detected isoforms, 1 and 2. The expression analysis of the two isoforms showed a marked difference when castes were compared, suggesting that they could be involved differently in the JH metabolism in M. scutellaris , providing new insights for the comprehension of female plasticity. Arch. Insect Biochem. Physiol. 2007. © 2007 Wiley‐Liss, Inc.