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ABSTRACT: Background
Argonaute (Ago) proteins interact with small regulatory RNAs to mediate gene regulatory pathways. A recent report by Kiriakidou et al. 1 describes an MC sequence region identified in Ago2 that displays similarity to the cap-binding motif in translation initiation factor 4E (eIF4E). In a cap-bound eIF4E structure, two important aromatic residues of the motif stack on either side of a 7-methylguanosine 5'-triphosphate (m7Gppp) base. The corresponding Ago2 aromatic residues (F450 and F505) were hypothesized to perform the same cap-binding function. However, the detected similarity between the MC sequence and the eIF4E cap-binding motif was questionable.Results
A number of sequence-based and structure-based bioinformatics methods reveal the reported similarity betwee
SUBMITTER: Kinch LN
PROVIDER: S-EPMC2636766 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature