Sequence and evolutionary analysis of bacterial ribosomal S1 proteins

Abstract

The multi-domain bacterial S1 protein is the largest and most functionally important ribosomal protein of the 30S subunit, which interacts with both mRNA and proteins. The family of ribosomal S1 proteins differs in the classical sense from a protein with tandem repeats and has a “bead-on-string” organization, where each repeat is folded into a globular domain. Based on our recent data, the study of evolutionary relationships for the bacterial phyla will provide evidence for one of the proposed theories of the evolutionary development of proteins with structural repeats: from multiple repeats of assembles to single repeats, or vice versa. In this comparative analysis of 1333 S1 sequences that were identified in 24 different phyla; we demonstrate how such phyla can independently/dependently form during evolution. To our knowledge, this work is the first study of the evolutionary history of bacterial ribosomal S1 proteins. The collected and structured data can be useful to computer biologists as a resource for determining percent identity, amino acid composition and logo motifs, as well as dN/dS ratio in bacterial S1 protein. The obtained research data suggested that the evolutionary development of bacterial ribosomal proteins S1 evolved from multiple assemblies to single repeat. The presented data are integrated into the server, which can be accessed at http://oka.protres.ru:4200.

Evaluation of the bacterial ribosomal protein S1 gene (rpsA) from the position of structural repetition

“…The family of bacterial ribosomal S1 proteins (rpsA) with repetitive S1 domains differs in a canonical sense from other similar proteins [1]. The S1 protein is essential for cell viability because it interacts with both mRNA and proteins.…”