Identification of residues of the archaeal RNA-binding Nip7 proteins specific to environmental conditions

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3 Citations (Scopus)

Abstract

The understanding of biological and molecular mechanisms providing survival of cells under extreme temperatures and pressures will help to answer fundamental questions related to the origin of life and to design of biotechnologically important enzymes with new properties. Here, we analyze amino acid sequences of the Nip7 proteins from 35 archaeal species to identify positions containing mutations specific to the hydrostatic pressure and temperature of organism's habitat. The number of such positions related to pressure change is much lower than related to temperature change. The results suggest that adaptation to temperature changes of the Nip7 protein cause more pronounced modifications in sequence and structure, than to the pressure changes. Structural analysis of residues at these positions demonstrated their involvement in salt-bridge formation, which may reflect the importance of protein structure stabilization by salt-bridges at extreme environmental conditions.

Original languageEnglish
Article number1650036
Pages (from-to)1650036
Number of pages18
JournalJournal of Bioinformatics and Computational Biology
Volume15
Issue number2
DOIs
Publication statusPublished - 1 Apr 2017

Keywords

  • archaea
  • extremophiles
  • high pressure
  • Nip7 protein
  • specificity determining positions
  • Adaptation, Physiological
  • Catalytic Domain
  • Temperature
  • RNA-Binding Proteins/chemistry
  • Models, Molecular
  • Sequence Homology, Amino Acid
  • Archaeal Proteins/chemistry
  • Amino Acid Substitution
  • SP-NOV REPRESENTS
  • HYPERTHERMOPHILIC ARCHAEON
  • ARCHAEBACTERIA
  • SEA HYDROTHERMAL VENT
  • METHANE-PRODUCING ARCHAEON
  • PRESSURE
  • SP. NOV.
  • COMPLETE GENOME SEQUENCE
  • DEEP
  • TEMPERATURE

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