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. 2019 Nov 7;294(50):19167–19183. doi: 10.1074/jbc.RA119.010686

Table 2.

Interaction of YidC with periplasmic chaperones and leader peptidase

A non-UV–irradiated (not cross-linked, −UV) and a UV-irradiated (cross-linked, +UV) sample of YidC(K249pBpa) purified from whole cells was separated on a 5–15% SDS gel, and the proteins were visualized by Coomassie staining. The −UV and the +UV lanes were cut into equal slices followed by in-gel trypsin digestion and mass spectrometry. Shown are the quantification for PpiD, Skp, FkbA, and LepB.

YidC(K249pBpa) in vivo cross-links
Proteina Molecular massb Gel molecular massc Relative intensity (−UV/+UV)d Coveragee Peptidesf
kDa kDa %
PpiD 68.1 168 0.02 48.6 24
Skp 16 79 0.00 37.3 7
FkbA 28.9 116 0.00 3.7 1
LepB 35.9 133 0.00 36.7 13

a This is the protein identified.

b This is the calculated molecular mass.

c The molecular mass of the gel slice was determined by extrapolation.

d The relative intensity observed in gel slices from the control lane (−UV) compared with the +UV lane is shown.

e The sequence coverage of the total sequence was by detected peptides.

f This is the number of peptides detected.