Identification of residues of the archaeal RNA-binding Nip7 proteins specific to environmental conditions.
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.
* Department of Biophysics, University of Texas Southwestern, Medical Center, Dallas, Texas 75390, USA.|† Institute of Cytology and Genetics Siberian Branch of the Russian Academy of Sciences, Prospekt Lavrentyeva 10, Novosibirsk 630090, Russia.
Kirill E
http://orcid.org/0000-0002-7982-4242
KE
Medvedev
† Institute of Cytology and Genetics Siberian Branch of the Russian Academy of Sciences, Prospekt Lavrentyeva 10, Novosibirsk 630090, Russia.|‡ NRC Kurchatov Institute, Akademika Kurchatova pl., 1, Moscow 123182, Russia.|§ Novosibirsk State University, Pirogova str. 2, Novosibirsk 630090, Russia.
Nikolay A
NA
Kolchanov
† Institute of Cytology and Genetics Siberian Branch of the Russian Academy of Sciences, Prospekt Lavrentyeva 10, Novosibirsk 630090, Russia.|§ Novosibirsk State University, Pirogova str. 2, Novosibirsk 630090, Russia.
Dmitry A
DA
Afonnikov
D000222:Adaptation, Physiological; D019943:Amino Acid Substitution; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D008958:Models, Molecular; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D019843:Archaeal Proteins; D016601:RNA-Binding Proteins
Nip7 protein; archaea; extremophiles; high pressure; specificity determining positions