Structural characterization of a protein pheromone from a cold‐adapted (Antarctic) single‐cell eukaryote, the ciliate Euplotes nobilii

FEBS Letters

Carratore, Vito¹  Luporini, Pierangelo²  Alimenti, Claudio²  Ortenzi, Claudio² 

[1] Istituto di Biochimica delle Proteine ed Enzimologia, CNR/IBPE, Via G. Marconi, 80125 Napoli, Italy;Dipartimento di Biologia Molecolare Cellulare e Animale, University of Camerino, 62032 Camerino (MC), Italy

关键词: Cold-adapted protein;    Glycine-rich motif;    Chemical cell signal;    Ciliate mating type;    Antarctic biology;    DTT;    dithiothreitol;    RP-HPLC;    reverse-phase high performance liquid chromatography;   

DOI  :  10.1016/S0014-5793(02)02393-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Free-living species of ciliated Protozoa control their vegetative (mitotic) proliferation and mating (sexual) processes by diffusible, cell type-specific protein signals (pheromones). One of these molecules, designated En-2, was isolated from a species, Euplotes nobilii, living in the stably cold marine waters of Antarctica, and its complete amino acid sequence of 60 residues was determined by automated Edman degradation of the whole protein and peptides generated by trypsin digestion. The proposed sequence is: DIEDFYTSETCPYKNDSQLA₂₀WDTCSGGTGNCGTVCCGQCF₄₀SFPVSQSCAGMADSNDCPNA₆₀. The En-2 structure appears to be characterized by an adaptive insertion of a glycine-rich motif potentially capable to confer more flexibility to a functionally critical region of the molecule.

【 授权许可】

Unknown