Hosokawa N, Takechi H, Yokota S, Hirayoshi K, Nagata K
Department of Cell Biology, Kyoto University, Japan.
Gene. 1993 Apr 30;126(2):187-93. doi: 10.1016/0378-1119(93)90366-b.
HSP47, a 47-kDa heat-shock protein (HSP), is a member of a group of HSPs with the unique characteristics of collagen binding as well as transformation sensitivity. The protein belongs to the serpin (serine protease inhibitor) superfamily as determined from its amino acid sequence homology. We have isolated and characterized the mouse HSP47 including about 1 kb of the 5'-flanking region. This gene spans about 7.8 kb, consisting of six exons separated by five introns. This exon-intron structure is different from other serpin family proteins. Southern blot analysis revealed the existence of a single copy of HSP47. The promoter region contains a TATA box, four Sp1-binding sites and one AP-1-binding site. A complete heat-shock element (HSE) was found between nucleotides (nt) -61 and -79. Furthermore, the heat inducibility was reproduced by transfecting mouse BALB/3T3 cells with a plasmid carrying cat under the control of the HSE-containing fragment (nt -197 and +38) of HSP47. Computer analysis of the promoter region did not show marked homology to other vertebrate promoters.
热休克蛋白47（HSP47）是一种47千道尔顿的热休克蛋白（HSP），是具有胶原蛋白结合以及转化敏感性独特特征的一组热休克蛋白成员。根据其氨基酸序列同源性确定，该蛋白属于丝氨酸蛋白酶抑制剂（serpin）超家族。我们已经分离并鉴定了小鼠HSP47，包括约1 kb的5'侧翼区域。该基因跨度约7.8 kb，由六个外显子和五个内含子分隔组成。这种外显子-内含子结构与其他丝氨酸蛋白酶抑制剂家族蛋白不同。Southern印迹分析显示HSP47存在单拷贝。启动子区域包含一个TATA盒、四个Sp1结合位点和一个AP-1结合位点。在核苷酸（nt）-61和-79之间发现了一个完整的热休克元件（HSE）。此外，通过用携带在HSP47的含HSE片段（nt -197和+38）控制下的氯霉素乙酰转移酶（cat）的质粒转染小鼠BALB/3T3细胞，重现了热诱导性。对启动子区域的计算机分析未显示与其他脊椎动物启动子有明显同源性。
