Research output: Contribution to journal › Article › peer-review
Identification of residues of the archaeal RNA-binding Nip7 proteins specific to environmental conditions. / Medvedev, Kirill E.; Kolchanov, Nikolay A.; Afonnikov, Dmitry A.
In: Journal of Bioinformatics and Computational Biology, Vol. 15, No. 2, 1650036, 01.04.2017, p. 1650036.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Identification of residues of the archaeal RNA-binding Nip7 proteins specific to environmental conditions
AU - Medvedev, Kirill E.
AU - Kolchanov, Nikolay A.
AU - Afonnikov, Dmitry A.
PY - 2017/4/1
Y1 - 2017/4/1
N2 - 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.
AB - 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.
KW - archaea
KW - extremophiles
KW - high pressure
KW - Nip7 protein
KW - specificity determining positions
KW - Adaptation, Physiological
KW - Catalytic Domain
KW - Temperature
KW - RNA-Binding Proteins/chemistry
KW - Models, Molecular
KW - Sequence Homology, Amino Acid
KW - Archaeal Proteins/chemistry
KW - Amino Acid Substitution
KW - SP-NOV REPRESENTS
KW - HYPERTHERMOPHILIC ARCHAEON
KW - ARCHAEBACTERIA
KW - SEA HYDROTHERMAL VENT
KW - METHANE-PRODUCING ARCHAEON
KW - PRESSURE
KW - SP. NOV.
KW - COMPLETE GENOME SEQUENCE
KW - DEEP
KW - TEMPERATURE
UR - http://www.scopus.com/inward/record.url?scp=84994718785&partnerID=8YFLogxK
U2 - 10.1142/S0219720016500360
DO - 10.1142/S0219720016500360
M3 - Article
C2 - 27832721
AN - SCOPUS:84994718785
VL - 15
SP - 1650036
JO - Journal of Bioinformatics and Computational Biology
JF - Journal of Bioinformatics and Computational Biology
SN - 0219-7200
IS - 2
M1 - 1650036
ER -
ID: 10036493