TY - JOUR
T1 - Dimerization of hepatitis B viral X protein synthesized in a cell-free system
AU - Lin, Meei Hua
AU - Lo, Szecheng J.
PY - 1989/10/16
Y1 - 1989/10/16
N2 - Hepatitis B viral X protein (HBx), a 17-kDa polypeptide, has been demonstrated as a trans-acting factor. In this study, we report that the HBx was able to form a dimer, a feature very similar to many well known trans-acting factors. In vitro synthesized HBx, after immunoprecipitation and analysis by SDS-PAGE, appeared as one prominent 17-kDa band (monomer) and a faint 34-kDa band (dimer). The amount of dimer increased if the sample of immunoprecipitated HBx was not treated with 2-mecaptoethanol, indicating the dimer was held together by the disulfide linkage. Dimerization of a truncated HBx established that the four cysteine residues close to the N-terminus are sufficient for the dimerization process.
AB - Hepatitis B viral X protein (HBx), a 17-kDa polypeptide, has been demonstrated as a trans-acting factor. In this study, we report that the HBx was able to form a dimer, a feature very similar to many well known trans-acting factors. In vitro synthesized HBx, after immunoprecipitation and analysis by SDS-PAGE, appeared as one prominent 17-kDa band (monomer) and a faint 34-kDa band (dimer). The amount of dimer increased if the sample of immunoprecipitated HBx was not treated with 2-mecaptoethanol, indicating the dimer was held together by the disulfide linkage. Dimerization of a truncated HBx established that the four cysteine residues close to the N-terminus are sufficient for the dimerization process.
UR - https://www.scopus.com/pages/publications/0024431955
U2 - 10.1016/0006-291X(89)91676-8
DO - 10.1016/0006-291X(89)91676-8
M3 - 文章
C2 - 2803288
AN - SCOPUS:0024431955
SN - 0006-291X
VL - 164
SP - 14
EP - 21
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -
