In silico identification of BESS-DC genes and expression analysis in the silkworm, Bombyx mori

Gene. 2016 Jan 10;575(2 Pt 2):478-487. doi: 10.1016/j.gene.2015.09.024. Epub 2015 Sep 16.

Abstract

BESS domain is a protein binding domain that can interact each other or with other domains. In this study, 323 BESS domain containing (BESS-DC) proteins were identified in 3328 proteomes. These BESS-DC genes pertain to 41 species of five phyla, most of which are arthropod insects. A BESS domain contains two α-helixes linked by a coil or β-turn. Phylogenetic tree and architecture analysis show that the BESS domain seems to generate along with the DNA-binding MADF domain. Two hundred thirty three BESS-DC genes (71.1%) contain at least one MADF domain, while 59 genes (18.2%) had only the BESS domain. In addition to BESS and MADF domains, some of genes also contain other ligand binding domains, such as DAO, DUS and NAD_C. Nineteen genes (5.8%) are associated with other DNA binding domains, such as Myb and BED. The BESS-DC genes can be divided into 17 subfamilies, eight of which have more than one clade. In Bombyx mori, 12 BESS-DC genes that do not contain intron in the BESS domain region were localized to eight chromosomes. Real-time PCR results showed that most of the B. mori BESS-DC genes highly expressed from late larval stage to adult stage. The results of sequence comparison and evolution analyses suggest a hypothesis that the BESS-DC genes may play a role in central nervous system development, long term memory and metamorphosis of insects of different phyla.

Keywords: BESS domain; Bioinformatics; Bombyx mori; Expression; Protein–protein interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Bombyx / genetics*
  • Chromosome Mapping
  • Chromosomes, Insect / genetics*
  • Computer Simulation
  • Gene Expression Profiling / methods*
  • Insect Proteins / chemistry*
  • Insect Proteins / classification
  • Insect Proteins / genetics*
  • Phylogeny
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary

Substances

  • Insect Proteins