Journal of Microbial & Biochemical Technology

Possible ancient motif in various bacterial proteins

Joint Event on 4^th World Congress and Expo on Applied Microbiology & 2^nd International Conference on Food Microbiology

November 29-December 01, 2017 Madrid, Spain

Skoblikow N E and Zimin A A

CL Medical Laboratory, Russia
North Caucasian Research Institute of Animal Husbandry, Russia
G K Skryabin Institute of Biochemistry and Physiology of Microorganisms �?? RAS, Russia

Posters & Accepted Abstracts: J Microb Biochem Technol

Abstract:

The study presents the results of analysis of protein sequence database of bacteria, which revealed a presence of conservative peptide sequence in various functionally and phylogenetically differing conservative proteins from representatives of various taxa. All proteins described as important, universal and evolutionarily ancient for all cellular forms of life: 4 aminoacyltRNA synthetases (phenylalanyl, glycyl, alanyl, histidyl, methionyl, glutamyl), 3 ribosomal proteins (L7/L12, L18, L30), DNA-polymerase III (α-subunit), NAD-dependent DNA ligase A and 5 metabolic enzymes (carbamoyl phosphate synthase (large subunit �?? CPS_L), phosphoenolpyruvate synthase (PEPs), acetyl-CoA carboxylase (subunit A), dihydrolipoamide dehydrogenase, heterodisulfide reductase (subunit B). In the supposed hypothesis the fragment of ribosomal RNA (part of the A-site including stems H92, H90 and H93 of the peptidyl transferase center, PTC) translated from one of the potential reading frames was a source of genetic information for this sequence at the earliest stages of macromolecular evolution.