Molecular evolutionary and 3D protein structural analyses of Lactobacillus fermentum elongation factor Tu, a novel brain health promoting factor

Ong JS 1 , Liu YW 2 , Liong MT 1 , Choi SB 3 , Tsai YC 4 , Low WY 5

Affiliations 

  • 1 Bioprocess Technology, School of Industrial Technology, Universiti Sains Malaysia, 11800 Penang, Malaysia
  • 2 Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan
  • 3 School of Data Sciences, Perdana University, Jalan MAEPS Perdana, 43400 Serdang, Selangor, Malaysia
  • 4 Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan. Electronic address: [email protected]
  • 5 School of Data Sciences, Perdana University, Jalan MAEPS Perdana, 43400 Serdang, Selangor, Malaysia; The Davies Research Centre, School of Animal and Veterinary Sciences, University of Adelaide, Roseworthy, SA 5371, Australia. Electronic address: [email protected]
Genomics, 2020 11;112(6):3915-3924.
PMID: 32629096 DOI: 10.1016/j.ygeno.2020.06.052

Abstract

The role of microbiota in gut-brain communication has led to the development of probiotics promoting brain health. Here we report a genomic study of a Lactobacillus fermentum PS150 and its patented bioactive protein, elongation factor Tu (EF-Tu), which is associated with cognitive improvement in rats. The L. fermentum PS150 circular chromosome is 2,238,401 bp and it consists of 2281 genes. Chromosome comparisons with other L. fermentum strains highlighted a cluster of glycosyltransferases as potential candidate probiotic factors besides EF-Tu. Molecular evolutionary analyses on EF-Tu genes (tuf) in 235 bacteria species revealed one to three copies of the gene per genome. Seven tuf pseudogenes were found and three species only possessed pseudogenes, which is an unprecedented finding. Protein variability analysis of EF-Tu showed five highly variable residues (40 K, 41G, 42 L, 44 K, and 46E) on the protein surface, which warrant further investigation regarding their potential roles as binding sites.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

MeSH terms
Similar publications