Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0624620100430050355
BMB Reports
2010 Volume.43 No. 5 p.355 ~ p.361
SAMD4B, a novel SAM-containing protein, inhibits AP-1-, p53- and p21-mediated transcriptional activity
Luo Na

Li Guan
Li Yong-Qing
Fan Xiong-Wei
Wang Yue-Qun
Ye Xian-Gli
Mo Xiao-Yan
Zhou Jun-Mei
Yuan Wu-Zhou
Tan Ming
Xie Hua-Ping
Ocorr Karen
Bodmer Rolf
Deng Yun
Wu Xiu-Shan
Abstract
The sterile alpha motif (SAM) is a putative protein interaction domain involved in a wide variety of biological processes. Here we report the identification and characterization of a novel gene, SAMD4B, which encodes a putative protein of 694 amino acids with a SAM domain. Northern blot and RT-PCR analysis showed that SAMD4B is widely expressed in human embryonic and adult tissues. Transcriptional activity assays show SAMD4B suppresses transcriptional activity of L8G5-luciferase. Over-expression of SAMD4B in mammalian cells inhibited the transcriptional activities of activator protein-1 (AP-1), p53 and p21, and the inhibitory effects can be relieved by siRNA. Deletion analysis indicates that the SAM domain is the main region for transcriptional suppression. The results suggest that SAMD4B is a widely expressed gene involved in AP-1-, p53-and p21-mediated transcriptional signaling activity.
KEYWORD
AP-1, p21, p53, SAMD4B, SAM protein
FullTexts / Linksout information
Listed journal information
SCI(E) ÇмúÁøÈïÀç´Ü(KCI) ´ëÇÑÀÇÇÐȸ ȸ¿ø