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. 1997 Jan 21;94(2):485–490. doi: 10.1073/pnas.94.2.485

Table 1.

Summary and quantification of crosslinking with pb2(220)-DHFR and pb2Δ19(220)-DHFR

Position* pb2(220)-DHFR crosslinking, %
pb2Δ19(220)-DHFR crosslinking, %
To Tom40 To Tim44 To Ssc1p To X To Tom40 To Tim44 To Ssc1p
86
94 i ≈10
114 i ≈ 3
123
132 ND ND ND
154 ND ND ND ND
162 i ≈ 10 i ≈ 3
183 i ≈ 10 ND ND ND
186 i ≈ 10
m ≈ 10§
195 i ≈ 5 i ≈ 5
m ≈ 5§
204 ? 5–10
213 i ≈ 4 i ≈ 2
m ≈ 3§

The radioactivity in the bands was quantified with image-analyzing system BAS2000 (Fuji Film). The radioactivity before crosslinking in the intermediate-size or the mature-size forms of the fusion proteins from which crosslinked products arose was taken as 100%. −, No crosslinking was detected; i, the intermediate-size form; m, the mature-size form. ND, crosslinking was not detected because of low efficiencies of suppression or the accumulation of translocating intermediates. The data for positions 106, 142, and 174 are all ND and are therefore omitted from the table. 

*

Position, residue number of introduced 2

The crosslinked products arose from the intermediate-size forms of the fusion proteins, since the presence of metal chelators (5 mM EDTA + 1 mM o-phenanthroline) caused a shift of the band to higher molecular mass by more than ≈3 kDa or changed the band into a smear. 

The crosslinked products arose from the intermediate-size forms of the fusion proteins, since the presence of metal chelators caused a shift of the band to higher molecular mass by ≈3 kDa. 

§

The crosslinked products arose from the mature-size form of the fusion protein since, it appeared just below the one arising from the intermediate-size form.