Abstract:

Objective: To analyze the structure and function of mitochondrial transcription termination factor DmTTF protein in
Drosophila melanogaster based on bioinformatics method. Methods: Based on the amino acid sequence of mitochondrial transcription
termination factor DmTTF protein in D. melanogaster from FlyBase database, the protein physicochemical property, hydrophilicity/
hydrophobicity, subcellular localization, secondary protein structure, protein domain, protein tertiary structure, protein- protein
interaction, as well as the protein evolution relationship of different species were analyzed by using different bioinformatics software.
Results: The mitochondrial transcription termination factor DmTTF protein consists of 410 amino acids, the estimated theoretical
molecular weight and is oelectric point were 48.3 kDa and 9.62 respectively, which belong to the MTERF protein superfamily without
transmembrane region, and it is a hydrophilic protein. The main composition of the DmTTF protein secondary structure were α-helix
and random coil, showed similar result with protein tertiary structure whose spatial structure and the coverage of template protein
3mvb.1.A was 74.0%. Proteins that interact with DmTTF were mitochondrial transcription factors or mitochondrial respiratory chain
proteins. DmTTF protein in D. melanogaster and encoded homologous protein in Musca demestica and Anopheles darlingi showed highly
homology. Conclusion: DmTTF protein in D. melanogaster contained the typical structure of mitochondrial transcription termination
factor protein family, which might involve in the transcription regulation of mitochondrial gene of D. melanogaster.

Key words: Drosophila melanogaster, mitochondrial transcription termination factor, bioinformatics, structure and function