In‐depth analysis of amino acid and nucleotide sequences of Hsp60: How conserved is this protein?

Abstract

Chaperonin Hsp60, as a protein found in all organisms, is of great interest in medicine, since it is present in many tissues and can be used both as a drug and as an object of targeted therapy. Hence, Hsp60 deserves a fundamental comparative analysis to assess its evolutionary characteristics. It was found that the percent identity of Hsp60 amino acid sequences both within and between phyla was not high enough to identify Hsp60s as highly conserved proteins. However, their ATP binding sites are largely conserved. The amino acid composition of Hsp60s remained relatively constant. At the same time, the analysis of the nucleotide sequences showed that GC content in the Hsp60 genes was comparable to or greater than the genomic values, which may indicate a high resistance to mutations due to tight control of the nucleotide composition by DNA repair systems. Natural selection plays a dominant role in the evolution of Hsp60 genes. The degree of mutational pressure affecting the Hsp60 genes is quite low, and its direction does not depend on taxonomy. Interestingly, for the Hsp60 genes from Chordata, Arthropoda, and Proteobacteria the exact direction of mutational pressure could not be determined. However, upon further division into classes, it was found that the direction of the mutational pressure for Hsp60 genes from Fish differs from that for other chordates. The direction of the mutational pressure affects the synonymous codon usage bias. The number of high and low represented codons increases with increasing GC content, which can improve codon usage. Special server has been created for bioinformatics analysis of Hsp60: http://oka.protres.ru:4202/.

Recombinant 60-kDa heat shock protein from Paracoccidioides brasiliensis induces the death of mouse lymphocytes in a mechanism dependent on Toll-like receptor 4 and tumor necrosis factor

“…HSP60s are molecules highly conserved in the evolution [ 7 ] and have been related to proinflammatory effects and apoptosis through binding to TLR4 [ 19 ]. Based on these data, we supposed TLR signaling could be responsible for lymphocyte death triggered by rHSP60.…”

“…that are expressed in response to changes in temperature and other stressful conditions are the heat shock proteins (HSPs) [ 5 ]. HSPs are a class of highly conserved molecules with constitutive expression in cells of all living beings [ 6 , 7 ]. Usually, HSPs can be found inside the cell in different compartments, such as cytosol, mitochondria, chloroplasts, and nucleus [ 8 , 9 ].…”