Argonaute

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The Argonaute protein is the catalytic component of the RISC complex, central to the RNA-induced silencing in eukaryotic organisms [1]. It is found in all higher eukaryotes and it plays an important role in a variety of processes as diverse as embryonic development, cell diferentiation and transposon silencing. These proteins are evolutionarily conserved and can be divided in two subfamilies: Ago and Piwi. The first are ubiquitously expressed and interact with siRNAs or miRNAs to participate in post-transcriptional gene silencing, both by destabilizing mRNA or by repressing the translation event. Piwi proteins are generally restricted to the germ line and associate piRNAs to mediate silencing of mobile genetic elements [2].

Structural OrganisationStructural Organisation

There are two main structural features common to all Argonaute proteins: the Paz domain and the PIWI domain. Other structural features include the N domain and the Mid domain.

Paz Domain

The is responsible for

The Paz domain

Piwi Domain

X-ray structure of the entire human Argonaute2 protein (PDB 4EI1) at 2.3Å resolution

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Schirle NT, Macrae IJ. The Crystal Structure of Human Argonaute2. Science. 2012 Apr 26. PMID:22539551 doi:10.1126/science.1221551
  2. Hock J, Meister G. The Argonaute protein family. Genome Biol. 2008;9(2):210. Epub 2008 Feb 26. PMID:18304383 doi:10.1186/gb-2008-9-2-210

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João Rodrigues, Michal Harel, Joel L. Sussman, Alexander Berchansky