Molecular Cloning and Expression of an Estrogen Receptor-Related Receptor Gene in the Ant Polyrhachis vicina (Hymenoptera: Formicidae)

• Published in: Annals of the Entomological Society of America Vol. 102; no. 2; pp. 295 - 302
• Main Authors: Ouyang, Xia-Hui, Xi, Geng-Si, Bu, Cui-Ping, Wang, Hui-Li, Zhan, Guang-Jie, Hong, Feng
• Format: Journal Article
• Language: English
• Published: Oxford, UK Entomological Society of America 01-03-2009; Oxford University Press
• Subjects: 5′-/3′-rapid amplification of cDNA ends (RACE); amino acid sequences; Biological and medical sciences; complementary DNA; developmental stages; DNA-binding domains; Estrogen receptor-related receptor (ERR); estrogens; exons; Formicidae; Fundamental and applied biological sciences. Psychology; gene expression; genes; hormone receptors; Hymenoptera; insect castes; Insecta; introns; Invertebrates; molecular cloning; molecular sequence data; nuclear receptors; nucleotide sequences; open reading frames; PHYSIOLOGY, BIOCHEMISTRY, AND TOXICOLOGY; Polyrhachis vicina; real-time quantitative polymerase chain reaction (PCR); Systematics. Geographical distribution; real-time quantitative polymerase chain reaction (PCR); molecular cloning; Estrogen receptor-related receptor (ERR); Polyrhachis vicina; 5’-/3’-rapid amplification of cDNA ends (RACE); Formicidae; Insecta; Estrogen; 5'-/3'-rapid amplification of cDNA ends (RACE); Social insect; Formicoidea; Amplification; Polymerase chain reaction; Gene; Arthropoda; Race; Hymenoptera; Invertebrata; Aculeata
• ISSN: 0013-8746; 1938-2901
• DOI: 10.1603/008.102.0211

Estrogen receptor-related receptors (ERRs) belong to a subfamily of orphan nuclear receptors where the proteins are closely related to the estrogen receptors (ERs) in structure. ERR homologs have been found in many animals and play an important role in the regulation physiologic processes. We have isolated the ERR homolog, abbreviated as PvERR, from the ant Polyrhachis vicina Roger (Hymenoptera: Formicidae). The full-length cDNA of the PvERR gene is 1,918 bp, containing a 5′-untranslated region (5′-UTR) of 245 bp and a 3′-UTR of 368 bp. The open reading frame of 1,305 bp encodes a 434-amino acid protein. The PvERR gene is composed of eight exons and seven introns. The tertiary structure of both the DNA binding domain and the ligand binding domain (LBD) of PvERR belong to the α + β type. The LBD of PvERR is formed by 11 α-helices without H2, and it is similar to the mammalian ERRγ LBD of known crystal structure. Further investigation indicated the potential significance of PvERR in the regulation of development in P. vicina, due to its expression in different developmental periods and castes.