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. 2014 Mar 6;9:e28224. doi: 10.4161/psb.28224

Table 1. Protein–protein interaction matrix of REIL1, REIL2 proteins with A. thaliana homologs of the yeast proteins, Rlp24p, Rpl24Ap, Rpl24B, Arx1p, and Jjj1p.

Protein Name REIL1 REIL2          
Yeast homologs Rei1p Reh1p Rpl24Ap Rpl24Bp Rlp24p Arx1p Jjj1p
Gene Code At4g31420 At2g24500 At2g36620 At3g53020 At2g44860 At3g51800 At1g74250
Full Length              
REIL1 7.9 11.9 5.1 5.1 - a 10.3 14.1
REIL2 2.0 16.1 - 6.6 3.3 4.5 2.2
Partial REIL1              
ZF1/2-ZF3/4b 14.6 35.0 5.6 3.1 18.5 5.0 9.5
ZF3/4-CD1/2 6.6 2.5 4.0 3.9 5.9 4.5 6.5
CD1/2 5.4 8.9 3.1 5.4 5.5 3.9 9.5
Partial REIL2              
ZF1/2-ZF3/4 6.2 32.8 5.9 7.7 2.9 7.4 -
ZF3/4-CD1/2 8.9 - 4.9 7.4 13.3 4.6 -
CD1/2 3.0 9.1 5.2 6.3 3.2 2.3 -

Full-length REIL bait proteins and C- or N-terminal truncations, rows also see (Fig. 3), were tested against full-length prey proteins, columns, using the yeast 2-hybrid assay. Values represent α-galactosidase activity of strains containing the respectively tested pair of heterologously expressed proteins. The activity is expressed as percent relative to a positive control strain carrying the plasmids pGBKT7–53 and pGADT7-T (Table S1)a Few interactions tested negative and did not yield viable yeast strains (-). b The full and partial proteins were cloned in to the bait vector using specific primers (Table S2). The names of the truncated proteins indicate the retained zinc finger domains (ZF) and REIL-specific conserved domains (CD). The α-galactosidase activity was assayed spectrophotometrically on microtiter plates using 4–8 replications per combination and controls. The technical standard deviation of this assay was 3.5%.