TY - JOUR
T1 - High mobility group protein-B1 interacts with sterol regulatory element-binding proteins to enhance their DNA binding
AU - Najima, Yuho
AU - Yahagi, Naoya
AU - Takeuchi, Yoshinori
AU - Matsuzaka, Takashi
AU - Sekiya, Motohiro
AU - Nakagawa, Yoshimi
AU - Amemiya-Kudo, Michiyo
AU - Okazaki, Hiroaki
AU - Okazaki, Sachiko
AU - Tamura, Yoshiaki
AU - Iizuka, Yoko
AU - Ohashi, Ken
AU - Harada, Kenji
AU - Gotoda, Takanari
AU - Nagai, Ryozo
AU - Kadowaki, Takashi
AU - Ishibashi, Shun
AU - Yamada, Nobuhiro
AU - Osuga, Jun Ichi
AU - Shimano, Hitoshi
PY - 2005/7/29
Y1 - 2005/7/29
N2 - Sterol regulatory element-binding proteins (SREBPs) are transcription factors that are predominately involved in the regulation of lipogenic and cholesterogenic enzyme gene expression. To identify unknown proteins that interact with SREBP, we screened nuclear extract proteins with 35S-labeled SREBP-1 bait in Far Western blotting analysis. Using this approach, high mobility group protein-B1 (HMGB1), a chromosomal protein, was identified as a novel SREBP interacting protein. In vitro glutathione S-transferase pull-down and in vivo coimmunoprecipitation studies confirmed an interaction between HMGB1 and both SREBP-1 and -2. The protein-protein interaction was mediated through the helix-loop-helix domain of SREBP-1, residues 309-344, and the A box of HMGB1. Furthermore, an electrophoretic mobility shift assay demonstrated that HMGB1 enhances SREBPs binding to their cognate DNA sequences. Moreover, luciferase reporter analyses, including RNA interference technique showed that HMGB1 potentiates the transcriptional activities of SREBP in cultured cells. These findings raise the intriguing possibility that HMGB1 is potentially involved in the regulation of lipogenic and cholesterogenic gene transcription.
AB - Sterol regulatory element-binding proteins (SREBPs) are transcription factors that are predominately involved in the regulation of lipogenic and cholesterogenic enzyme gene expression. To identify unknown proteins that interact with SREBP, we screened nuclear extract proteins with 35S-labeled SREBP-1 bait in Far Western blotting analysis. Using this approach, high mobility group protein-B1 (HMGB1), a chromosomal protein, was identified as a novel SREBP interacting protein. In vitro glutathione S-transferase pull-down and in vivo coimmunoprecipitation studies confirmed an interaction between HMGB1 and both SREBP-1 and -2. The protein-protein interaction was mediated through the helix-loop-helix domain of SREBP-1, residues 309-344, and the A box of HMGB1. Furthermore, an electrophoretic mobility shift assay demonstrated that HMGB1 enhances SREBPs binding to their cognate DNA sequences. Moreover, luciferase reporter analyses, including RNA interference technique showed that HMGB1 potentiates the transcriptional activities of SREBP in cultured cells. These findings raise the intriguing possibility that HMGB1 is potentially involved in the regulation of lipogenic and cholesterogenic gene transcription.
UR - http://www.scopus.com/inward/record.url?scp=23044493944&partnerID=8YFLogxK
U2 - 10.1074/jbc.M414549200
DO - 10.1074/jbc.M414549200
M3 - 学術論文
C2 - 16040616
AN - SCOPUS:23044493944
SN - 0021-9258
VL - 280
SP - 27523
EP - 27532
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 30
ER -