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cDNA cloning of Clavanins: antimicrobial peptides of tunicate hemocytes
Author(s) -
Zhao Chengquan,
Liaw Lilian,
Hee Lee In,
Lehrer Robert I
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00646-7
Subject(s) - tunicate , signal peptide , peptide , complementary dna , residue (chemistry) , peptide sequence , biochemistry , biology , antimicrobial peptides , amino acid , chemistry , gene , ecology
Clavanins are a family of α‐helical antimicrobial peptides found in hemocytes of the tunicate, Styela clava . We examined a cDNA library prepared from pharyngeal tissues of S. clava and sequenced 24 clones that encoded prepropeptides of Clavanins A, C, D or E. These sequences indicated that Clavanins are synthesized as 9.2 kDa prepropeptides which contain a 19‐residue signal peptide, followed in turn by a highly polar ‘pro’ region (LEERKSEEEK) with five glutamic acid residues, the 23 residues of the mature Clavanin peptide, the glycine residue needed for its amidation and a 27‐residue polar C‐terminal extension that is removed in later processing. Although the signal sequence and anionic propiece of Clavanin precursors share features with corresponding regions in precursors of the certain frog peptides, including ranalexin, gaegurins, dermaseptins and deltorphins, their unique multipartite structure suggests that they are not actually homologues of these amphibian peptides.