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In-depth analysis of amino acid and nucleotide sequences of Hsp60: how conserved is this protein?
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  • Tatyana Tikhomirova,
  • Maxim Matyunin,
  • Mikhail Lobanov,
  • Oxana Galzitskaya
Tatyana Tikhomirova
1Institute for Biological Instrumentation, Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences”

Corresponding Author:[email protected]

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Maxim Matyunin
3 Institute of Protein Research, Russian Academy of Sciences
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Mikhail Lobanov
Institute of Protein Research
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Oxana Galzitskaya
Institute of Protein Research
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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. In turn, their amino acid composition 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.
10 Sep 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
13 Sep 2021Submission Checks Completed
13 Sep 2021Assigned to Editor
13 Sep 2021Reviewer(s) Assigned
13 Oct 2021Review(s) Completed, Editorial Evaluation Pending
14 Oct 2021Editorial Decision: Revise Major
05 Dec 20211st Revision Received
06 Dec 2021Assigned to Editor
06 Dec 2021Submission Checks Completed
07 Dec 2021Reviewer(s) Assigned
21 Dec 2021Review(s) Completed, Editorial Evaluation Pending
21 Dec 2021Editorial Decision: Revise Minor
21 Dec 20212nd Revision Received
22 Dec 2021Assigned to Editor
22 Dec 2021Submission Checks Completed
22 Dec 2021Review(s) Completed, Editorial Evaluation Pending
23 Dec 2021Editorial Decision: Accept
May 2022Published in Proteins: Structure, Function, and Bioinformatics volume 90 issue 5 on pages 1119-1141. 10.1002/prot.26294