SAMD4B, a novel SAM-containing protein, inhibits AP-1-, p53- and p21-mediated transcriptional activity

作者：Na Luo, Li Guan, Yongqing Li, Xiongwei Fan, Yuequn Wang, Xiangli Ye, Xiaoyan Mo, Junmei Zhou, Wuzhou Yuan, Ming Tan, Huaping Xie, Karen Ocorr, Rolf Bodmer, Yun Deng, Xiushan Wu · 发表于：BMB Reports · 年份：2010 · DOI：10.5483/bmbrep.2010.43.5.355 · 被引用次数：18 · 研究领域：Ubiquitin and proteasome pathways、14-3-3 protein interactions、Peptidase Inhibition and Analysis

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.