Dimerization of hepatitis B viral X protein synthesized in a cell-free system

Meei Hua Lin; Szecheng J. Lo

doi:10.1016/0006-291X(89)91676-8

Dimerization of hepatitis B viral X protein synthesized in a cell-free system

Meei Hua Lin
, Szecheng J. Lo^*

^*Corresponding author for this work

National Yang Ming Chiao Tung University

Research output: Contribution to journal › Journal Article › peer-review

26 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	14-21
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	164
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(89)91676-8
State	Published - 16 10 1989
Externally published	Yes

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SDG 3 Good Health and Well-being

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10.1016/0006-291X(89)91676-8

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title = "Dimerization of hepatitis B viral X protein synthesized in a cell-free system",

abstract = "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.",

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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

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DO - 10.1016/0006-291X(89)91676-8

M3 - 文章

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AN - SCOPUS:0024431955

SN - 0006-291X

VL - 164

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EP - 21

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Dimerization of hepatitis B viral X protein synthesized in a cell-free system

Abstract

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