Expression, purification and characterization of TMCO1 for structural studies.

Abstract:

:Transmembrane and coiled-coil domains 1 (TMCO1) has a highly conserved amino acid sequence among species, indicating a critical role of TMCO1 in cell physiology. The deficiency of TMCO1 in humans is associated with cerebrofaciothoracic dysplasia (CFTD), glaucoma, osteogenesis and the occurrence of cancer. TMCO1 was recently identified as an endoplasmic reticulum (ER) Ca2+ load-activated Ca2+ (CLAC) release channel, which prevents ER Ca2+ overload and maintains calcium homeostasis in the ER. However, the structural basis of the molecular function of TMCO1 channel remains elusive. To determine the structure of TMCO1, we screened the expression of TMCO1 in Escherichia coli and insect cell expression systems. TMCO1 from Dictyostelium discoideum (DdTMCO1) was successfully expressed in Escherichia coli with a high yield. The pure recombinant protein was obtained by affinity chromatography and size exclusion chromatography. The solution NMR of DdTMCO1 in DPC micelles showed three α-helical transmembrane regions.

journal_name

Protein Expr Purif

authors

Zhang N,Tang M,Wen M,Cao Y,OuYang B

doi

10.1016/j.pep.2020.105803

subject

Has Abstract

pub_date

2021-03-01 00:00:00

pages

105803

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(20)30394-6

journal_volume

179

pub_type

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