Bioinformatics analysis of microalgal lipid droplet proteins

Le résumé fourni par la source

The experiment was to explore the structural features of microalgal lipid droplet proteins. Bioinformatics methods were used to investigate the physicochemical properties, hydrophilicity/hydrophobicity, signal peptide, transmembrane domain, amphipathic α-helix, secondary structure, domain, tertiary structure, conserved motif and phosphorylation sites of microalgal lipid droplet proteins. The results showed that LDSP protein of Nannochloropsis was a stable basic hydrophobin without signal peptide. The two transmembrane domains formed amphiphilic α-helix and hydrophobic α-helix, respectively. The secondary structure consisted of α-helix, extended chain, β-turn and random coil. It had a middle domain of thiamine pyrophosphate, a funnel-shaped tertiary structure, a conserved motif at C-terminus, which has nine phosphorylation sites. Unlike LDSP protein of Nannochloropsis, MLDP protein of Dunaliella pavus and HOGP protein of Haematococcus pluvialis were acidic hydrophilic proteins without transmembrane domain, and the sequences interacting with membrane formed amphiphilic α-helices. They had the rubber elongation factor domain, a dumbbell-shaped tertiary structure, 33 and 24 phosphorylation sites respectively. The structural features of MLDP protein of Chlamydomonas reinhardtii were between two types of features. The study indicates that the structures of microalgal lipid droplet proteins are differentiated, which might lead to differences in function.

Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.