Table 2 PGRMC1 proteins exhibit haem-dependent dimerization in solution.

From: Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance

 

Apo form

Haem-bound form

  

Mass (Da)

 

Mass (Da)

a PGRMC1 wt (a.a.44–195)

 ESI-MS

—

17,844.14

—

36,920.19

 Theoretical

 

17,843.65

 

36,918.06

 

Hydrodynamic radius 10−9 (m)

MW (kDa)

Hydrodynamic radius 10−9 (m)

MW (kDa)

 DOSY

2.04–2.15

20

2.94–3.02

42

 

S20,w (S)

MW (kDa)

S20,w (S)

MW (kDa)

 SV-AUC

1.9

17.6

3.1

35.5

b PGRMC1 C129S (a.a.44–195)

 ESI-MS

—

17,827.91

—

36,887.07

 Theoretical

 

17,827.59

 

36,885.6

 

S20,w (S)

MW (kDa)

S20,w (S)

MW (kDa)

 SV-AUC

2.0

18.1

3.1

35.8

  1. Differences in molecular weights of the wild-type (wt; a) and the C129S mutant (b) PGRMC1 proteins in the absence (apo form) or the presence of haem (haem-bound form). The protein sizes of the wt and C129S PGRMC1 cytosolic domains (a.a.44–195) in the presence or absence of haem were estimated by ESI-MS, DOSY and SV-AUC.
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