A full length amphioxus cDNA, encoding a novel phosducin-like protein （Amphi-PhLP）, was identified for the first time from the gut cDNA library of Branchiostoma belcheri. It is comprised of 1 550 bp and an open read...A full length amphioxus cDNA, encoding a novel phosducin-like protein （Amphi-PhLP）, was identified for the first time from the gut cDNA library of Branchiostoma belcheri. It is comprised of 1 550 bp and an open reading frame （ORF） of 241 amino acids, with a predicted molecular mass of approximately 28 kDa. In situ hybridization histochemistry revealed a tissue-specific expression pattern of Amphi-PhLP with the high levels in the ovary, and at a lower level in the hind grit and testis, hepatic caecum, gill, endostyle, and epipbaryngeal groove, while it was absent in the muscle, neural tube and notochord. In the Chinese Hamster Ovary （CHO） cells transfected with the expression plasmid pEGFP-NI/Amphi-PhLP, the fusion protein was targeted in the cytoplasm of CHO cells, suggesting that Amphi-PhLP is a cytosolic protein. This work may provide a framework for further understanding of the physiological function of Amphi-PhLP in B. belcheri.展开更多
基金Supported by the Pilot Projects of Knowledge Innovation Project of Chinese Academy of Sciences (No. KZCX2-YW-211-03 and MGE2008KG06)
文摘A full length amphioxus cDNA, encoding a novel phosducin-like protein （Amphi-PhLP）, was identified for the first time from the gut cDNA library of Branchiostoma belcheri. It is comprised of 1 550 bp and an open reading frame （ORF） of 241 amino acids, with a predicted molecular mass of approximately 28 kDa. In situ hybridization histochemistry revealed a tissue-specific expression pattern of Amphi-PhLP with the high levels in the ovary, and at a lower level in the hind grit and testis, hepatic caecum, gill, endostyle, and epipbaryngeal groove, while it was absent in the muscle, neural tube and notochord. In the Chinese Hamster Ovary （CHO） cells transfected with the expression plasmid pEGFP-NI/Amphi-PhLP, the fusion protein was targeted in the cytoplasm of CHO cells, suggesting that Amphi-PhLP is a cytosolic protein. This work may provide a framework for further understanding of the physiological function of Amphi-PhLP in B. belcheri.
