Molecular cloning and localization of a novel serine protease from the colonial tunicate Botryllus schlosseri.
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.
Müller
W E
WE
Institut für Physiologische Chemie, Universität, Mainz, Germany.
Pancer
Z
Z
Rinkevich
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D014561:Urochordata / Q000201:enzymology* / Q000235:genetics
D018076:DNA, Complementary; D012333:RNA, Messenger; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases