Argonaute: Difference between revisions
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===Paz Domain=== | ===Paz Domain=== | ||
The <scene name='Argonaute/Ago2-paz/1'>Paz Domain</scene> is responsible for binding to the 3'-end overhangs of single-stranded RNAs and siRNA duplexes <ref name='ref3'>pmid 15152257</ref> and was shown to be essential for RISC activation <ref name=' | The <scene name='Argonaute/Ago2-paz/1'>Paz Domain</scene> is responsible for binding to the 3'-end overhangs of single-stranded RNAs and siRNA duplexes <ref name='ref3'>pmid 15152257</ref> and was shown to be essential for RISC activation <ref name='ref4'>pmid 22795694</ref>. <scene name='Argonaute/Ago2-paz-obfold/2'>The domain is composed of two subdomains:</scene> the first is similar to the OB fold, a well known nucleic acid binding fold; the second subdomain is composed of a beta-hairpin followed by an alpha-helix. The cleft in between these two subdomains appears to interact with the 3' ends of ssRNA <ref name='ref5'>pmid 14615801</ref> (<scene name='Argonaute/Ago2-paz-binding-cleft/2'>See in structure</scene>) | ||
===Piwi Domain=== | ===Piwi Domain=== | ||
Revision as of 15:01, 6 September 2012
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 DomainThe is responsible for binding to the 3'-end overhangs of single-stranded RNAs and siRNA duplexes [3] and was shown to be essential for RISC activation [4]. the first is similar to the OB fold, a well known nucleic acid binding fold; the second subdomain is composed of a beta-hairpin followed by an alpha-helix. The cleft in between these two subdomains appears to interact with the 3' ends of ssRNA [5] () Piwi Domain |
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ReferencesReferences
- ↑ Schirle NT, Macrae IJ. The Crystal Structure of Human Argonaute2. Science. 2012 Apr 26. PMID:22539551 doi:10.1126/science.1221551
- ↑ 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
- ↑ Ma JB, Ye K, Patel DJ. Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature. 2004 May 20;429(6989):318-22. PMID:15152257 doi:10.1038/nature02519
- ↑ Gu S, Jin L, Huang Y, Zhang F, Kay MA. Slicing-Independent RISC Activation Requires the Argonaute PAZ Domain. Curr Biol. 2012 Aug 21;22(16):1536-42. Epub 2012 Jul 12. PMID:22795694 doi:10.1016/j.cub.2012.06.040
- ↑ Lingel A, Simon B, Izaurralde E, Sattler M. Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain. Nature. 2003 Nov 27;426(6965):465-9. Epub 2003 Nov 16. PMID:14615801 doi:10.1038/nature02123