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Structure

Length and domains

Primary Structure

The Ago1 protein has the same 4 primary domains as all argonaut (N, PAZ, Mid, PIWI, describe in the page Argonaut) and the two linker regions L1 (also called DUF1785 domain) and L2. Indeed, there is 84% of similitudes between the primary sequence of hAgo1 and hAgo2. Besides the N domain is interacting with L1, L2 and PIWI domains via residues 18-48 and 138-173.

Besides, Argonaut 1 can be found in a lot of phylogenetic groups, with different structure. For example, in the plant Brachypodium distachyon, where 10 argonauts proteins have been discovered, BdAGO1 lacks the N and Mid domains. This particularity explains the small size of this protein with only 624 residues. Moreover, BdAGO1 is related to Ago1 since the catalytic tetrad in the PIWI domain doesn’t work for it, enabling an endonuclease activity due to a missing of the last D/H residue

However, the AtAGO1 (from Arabidopsis thaliana), which can be find in the nucleus and the cytoplasm of the plant, owns a Mid domain and its conformation is homologous to BdAO9, BdAGO11, BdAGO12, BdAGO15, and BdAGO16. On the other hand, BdAGO1 has AtAGO4 as its closest homolog (like BaAGO2, BdAGO3 and BdAGO4), even if the AtAGO4 possess a Mid Domain.

Associated Proteins with Ago1

The Argonaute 1 protein can be associated with others molecular components of the cell. Therefore, proteomic analysis has demonstrated that RNase III Dicer binds hAgo1 through the PIWI domain (see page on argonaute) and also, at least, four other proteins in specific association with hAgo1:

• TNRC6B isoform 1 / KIAA1093 (175kDa) which has RRM motif at C-term to recognize RNA, and also GW repeats (trinucleotide motifs)

• MOV10 (130kDa)

• PRMT5 (arginine methyl-transferase) (70kDa)

• And, with more doubts, the translation factor eEF1α (50kDa)

Function

Disease

Relevance

Structural highlights

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