Evolutionary conservation of a unique amino acid sequence in human DICER protein essential for binding to Argonaute family proteins.
The Argonaute family and DICER proteins are major key proteins involved in the RNA-mediated gene silencing mechanism of various species. In this mechanism, cleavage of messenger RNAs (mRNA) or suppression of mRNA translation takes place via small RNAs that are uniquely processed by DICER. Previously, we demonstrated that human Argonaute family proteins bind to DICER. In this study, we identified a unique amino acid sequence of 127 amino acids in the RIBOc-A domain of human DICER protein as a "binding site" to Argonaute proteins. Comparative genomics analysis revealed that this unique amino acid sequence is highly conserved in the vertebrates, but not found in the non-vertebrate species. Significant difference in the RIBOc-A domain of DICER protein between vertebrate and non-vertebrate species may help exploring the functional complexity in the RNA-mediated gene silencing mechanism.
Sasaki
Takashi
T
Department of Molecular Biology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo, 160-8582, Japan.
Shimizu
Nobuyoshi
N
D000595:Amino Acid Sequence; D060565:Argonaute Proteins; D001665:Binding Sites; D039642:Eukaryotic Initiation Factors / Q000235:genetics*; D019143:Evolution, Molecular; D017353:Gene Deletion; D020868:Gene Silencing; D005822:Genetic Vectors; D023281:Genomics; D006801:Humans; D008954:Models, Biological; D008957:Models, Genetic; D008969:Molecular Sequence Data; D010802:Phylogeny; D043244:Ribonuclease III / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
C115848:AGO1 protein, human; D060565:Argonaute Proteins; D039642:Eukaryotic Initiation Factors; D043244:Ribonuclease III