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. Author manuscript; available in PMC: 2013 Jun 17.
Published in final edited form as: Nat Struct Mol Biol. 2011 Dec 18;19(1):90–97. doi: 10.1038/nsmb.2186

Table 1.

Comparative proteomic of ERI components

Gene Protein Structural Description # Independent Detection (% Peptide Coverage)

Common DCR-1, ERI-1 and ERI-5 Interactions ERI-51 ERI-1(FLAG)2 DCR-1(HA)2
Y38F2AR.1 ERI-5 (61.6) Tudor domain 5/5 (19) 2/2 (9) 3/3 (24)
F10B5.7 RRF-3 (201.4) RdRP 5/5 (12) 2/2 (15) 3/3 (24)
D2005.5 DRH-3 (129.1) DEAH/D box RNA helicase 4/5 (18) 2/2 (19) 3/3 (35)
K12H4.8 DCR-1 (210.9) DExH box RNA helicase/RNaseIII 4/5 (2) 2/2 (13) 3/3 (41)
T20G5.11 RDE-4 (43.4) dsRBD 1/5 (6) 2/2 (11) 3/3 (44)
W09B6.3 ERI-3 (66.4) Novel 1/5 (4) 2/2 (12) 3/3 (33)
T07A9.5b ERI-1b (67.2) SAP domain, exonuclease 1/5 (2) 2/2 (31) 2/3 (13)
T23G7.5 PIR-1 (30.1) RNA phosphatase 1/5 (7) 1/2 (8) 3/3 (47)

Common DCR-1 and ERI-1 Interactions

C26E6.7 ERI-9 (73.2) Novel nd 2/2 (7) 3/3 (7)
T06A10.3 (19.9) Novel nd 2/2 (11) 2/3 (8)
B0001.2 (105.1) Novel nd 2/2 (7) 2/3 (6)
T07D3.7 ALG-2 (101.6) Piwi/PAZ domain nd 2/2 (5) 3 W
F48F7.1 ALG-1 (110.9) Piwi/PAZ domain nd 2/2 (4) 3 W
1

Immunopurifications of ERI-5 were conducted using a covalently coupled polyclonal matrix. Since peptide coverage varied between independent samples, peptide coverage for the best ERI-5 recovery is used here.

2

Immunoprecipitations conducted on tagged proteins (Flag and HA, as indicated), expressed from null allele-rescuing transgenes(See Duchaine et al. 2006).

3

These two proteins were not detected in embryonic DCR-1 proteomic analyses, but were detected in adult purifications and with embryonic DCR-1 by western blotting (W).