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Archaeal and eukaryal translation initiation factor 1 differ in their RNA interacting loops
Author(s) -
Gogoi Prerana,
Kanaujia Shankar Prasad
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13044
Subject(s) - eukaryotic translation , translation (biology) , initiation factor , biology , open reading frame , computational biology , genetics , chemistry , peptide sequence , messenger rna , gene
The archaeal translation initiation factor 1 ( aIF 1) is reported to be functionally homologous to the eukaryotic translation initiation factor 1 ( eIF 1). However, lack of a structural comparison between aIF 1 and eIF 1 has limited our understanding of the structural (dis)similarities. Herein, we have determined the three‐dimensional crystal structure of an open reading frame PH 1771.1 encoding aIF 1 in Pyrococcus horikoshii OT 3. Results reveal that although aIF 1 has low sequence similarity with eIF 1, high structural homology exists between the two proteins. Nonetheless, notable critical differences between aIF 1 and eIF 1 could still be perceived at the β 1 –β 2 basic loop, the acidic loop and the solvent‐exposed surface. These differences might lead to a slightly divergent mode of action of aIF 1 during archaeal translation initiation.