Müller W E, Pancer Z, Rinkevich B
Institut für Physiologische Chemie, Universität, Mainz, Germany.
Mol Mar Biol Biotechnol. 1994 Apr;3(2):70-7.
A cDNA encoding a putative serine protease was isolated and characterized from Botryllus schlosseri, a colonial protochordate. The open-reading frame of the 846 bp cDNA is 744-nt long. The deduced aa sequence predicts a protein of 26,134 D, with the signature of chymotrypsin. The mRNA of the protease is expressed only in the zooids as a single 0.9-kb transcript. No transcript was found in the tunic matrix (test). Surprisingly, a 3.7-fold higher enzyme activity was found in the test, compared with the zooids. We propose that this serine protease may have a role as a biologically active compound in the defense mechanisms against epibionts or as part of the effector mechanisms expressed in allogeneic and xenogeneic interactions.
从群体原索动物柄海鞘中分离并鉴定出一个编码假定丝氨酸蛋白酶的cDNA。该846 bp cDNA的开放阅读框长744 nt。推导的氨基酸序列预测出一个26,134 D的蛋白质，具有胰凝乳蛋白酶的特征。该蛋白酶的mRNA仅在游动孢子中作为单一的0.9 kb转录本表达。在被囊基质（被囊）中未发现转录本。令人惊讶的是，与游动孢子相比，在被囊中发现的酶活性高3.7倍。我们认为这种丝氨酸蛋白酶可能作为一种生物活性化合物在抵抗体表寄生物的防御机制中发挥作用，或者作为同种异体和异种相互作用中表达的效应机制的一部分。
