A cysteine‐rich protein in the Theromyzon (Annelida: Hirudinea) cocoon membrane

FEBS Letters

Shain, Daniel H¹  Mason, Tarin A¹  McIlroy, Patrick J¹ 

[1] Biology Department, 315 Penn Street, Rutgers, The State University of New Jersey, Camden, NJ 08102, USA

关键词: Glossiphoniid leech;    Annelid;    Cysteine-rich;    Development;    Cocoon;    Egg capsule;   

DOI  :  10.1016/S0014-5793(04)00167-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The aquatic leech, Theromyzon rude, secretes a flexible, proteinaceous cocoon that is resistant to a broad range of denaturing conditions (e.g. heat, denaturing chemicals). We have partially solubilized the Theromyzon cocoon membrane in 10% acetic acid and identified two major protein fragments. Microsequencing of both Theromyzon cocoon protein (Tcp) fragments generated an identical stretch of the amino-terminal sequence that was used to clone the corresponding gene. The predicted linear amino acid sequence of the resulting cDNA contained an unusually high cysteine content (17.8%). Sequence analysis identified six internal repeats, each comprising 12 ordered Cys residues in a ∼62 amino acid repeating unit. Sequence comparisons identified homology with undescribed, Cys-rich repeats across animal phyla (i.e. Arthropod, Nematoda).

【 授权许可】

Unknown