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Structural modelling and phylogenetic analyses of PgeIF4A2 (Eukaryotic translation initiation factor) from Pennisetum glaucum reveal signature motifs with a role in stress tolerance and development.


ABSTRACT: Eukaryotic translation initiation factor 4A (eIF4A) is an indispensable component of the translation machinery and also play a role in developmental processes and stress alleviation in plants and animals. Different eIF4A isoforms are present in the cytosol of the cell, namely, eIF4A1, eIF4A2, and eIF4A3 and their expression is tightly regulated in cap-dependent translation. We revealed the structural model of PgeIF4A2 protein using the crystal structure of Homo sapiens eIF4A3 (PDB ID: 2J0S) as template by Modeller 9.12. The resultant PgeIF4A2 model structure was refined by PROCHECK, ProSA, Verify3D and RMSD that showed the model structure is reliable with 77 % amino acid sequence identity with template. Investigation revealed two conserved signatures for ATP-dependent RNA Helicase DEAD-box conserved site (VLDEADEML) and RNA helicase DEAD-box type, Q-motif in sheet-turn-helix and ?-helical region respectively. All these conserved motifs are responsible for response during developmental stages and stress tolerance in plants.

SUBMITTER: Agarwal A 

PROVIDER: S-EPMC5357570 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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Structural modelling and phylogenetic analyses of <i>PgeIF4A2</i> (Eukaryotic translation initiation factor) from <i>Pennisetum glaucum</i> reveal signature motifs with a role in stress tolerance and development.

Agarwal Aakrati A   Mudgil Yashwanti Y   Pandey Saurabh S   Fartyal Dhirendra D   Reddy Malireddy K MK  

Bioinformation 20161219 12


Eukaryotic translation initiation factor 4A (eIF4A) is an indispensable component of the translation machinery and also play a role in developmental processes and stress alleviation in plants and animals. Different eIF4A isoforms are present in the cytosol of the cell, namely, eIF4A1, eIF4A2, and eIF4A3 and their expression is tightly regulated in cap-dependent translation. We revealed the structural model of PgeIF4A2 protein using the crystal structure of Homo sapiens eIF4A3 (PDB ID: 2J0S) as t  ...[more]

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