Evolutionary conservation of a unique amino acid sequence in human DICER protein essential for binding to Argonaute family proteins

Takashi Sasaki, Nobuyoshi Shimizu

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)312-320
Number of pages9
JournalGene
Volume396
Issue number2
DOIs
Publication statusPublished - 2007 Jul 15

Fingerprint

Argonaute Proteins
Protein Binding
Amino Acid Sequence
Gene Silencing
RNA
Vertebrates
Messenger RNA
Proteins
Genomics
Binding Sites
Amino Acids

Keywords

  • Protein-protein interaction
  • RNAi

ASJC Scopus subject areas

  • Genetics

Cite this

Evolutionary conservation of a unique amino acid sequence in human DICER protein essential for binding to Argonaute family proteins. / Sasaki, Takashi; Shimizu, Nobuyoshi.

In: Gene, Vol. 396, No. 2, 15.07.2007, p. 312-320.

Research output: Contribution to journalArticle

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