Mameli M, Tuccini A, Mazza M, Petacchi R, Pelosi P
Istituto di Industrie Agrarie, University of Pisa, Italy.
Insect Biochem Mol Biol. 1996 Sep-Oct;26(8-9):875-82. doi: 10.1016/s0965-1748(96)00055-0.
Soluble proteins of low molecular weight have been purified from chemosensory organs of five species of Phasmids. On the basis of their N-terminal amino acid sequences, two classes can be identified. Polypeptides of 14 and 15 kDa, expressed in the antennae and legs of Eurycantha calcarata and Extatosoma tiaratum, as well as in the antennae of Carausius morosus, bear a close similarity (around 45% identity) with a soluble protein associated with the sensilla coeloconica of Drosophila melanogaster. Two proteins of 19 and 18 kDa, isolated from the antennae and the maxillary palpi, respectively, of Acrophylla wuelfingi, are 59 and 75% identical, in their N-terminal region, to a 19 kDa antennal protein of Carausius morosus. Similarity between members of the two classes is not significant, being limited to two to three identical amino acids in the most favorable cases. Finally, a 17 kDa protein, specifically expressed in the antennae of Sipyloidea sipylus, did not show any homology with other proteins. The expression in sensory organs and the characteristics of these proteins may suggest a function in chemosensory transduction.
已从五种竹节虫的化学感受器官中纯化出低分子量的可溶性蛋白质。根据它们的N端氨基酸序列，可以识别出两类。在巨棘刺腿竹节虫和皇冠竹节虫的触角和腿部以及葡萄胸针竹节虫的触角中表达的14 kDa和15 kDa多肽，与一种与黑腹果蝇的腔锥感器相关的可溶性蛋白质具有密切的相似性（约45%的同一性）。分别从武氏叶角竹节虫的触角和上颌触须中分离出的两种19 kDa和18 kDa的蛋白质，在其N端区域与葡萄胸针竹节虫的一种19 kDa触角蛋白的同一性分别为59%和75%。这两类成员之间的相似性并不显著，在最有利的情况下仅限于两到三个相同的氨基酸。最后，在西氏叶角竹节虫的触角中特异性表达的一种17 kDa蛋白质与其他蛋白质没有任何同源性。这些蛋白质在感觉器官中的表达及其特性可能表明它们在化学感受转导中发挥作用。
