STRUCTURE OF THE GENE ENCODING THE MOUSE 47-KDA HEAT-SHOCK PROTEIN (HSP47)

HSP47, a 47-kDa heat-shock protein (HSP), is a member of a group of HS Ps with the unique characteristics of collagen binding as well as tran sformation sensitivity. The protein belongs to the serpin (serine prot ease inhibitor) superfamily as determined from its amino acid sequence homology. We have isolated and characterized the mouse HSP47 includin g 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 st ructure is different from other serpin family proteins. Southern blot analysis revealed the existence of a single copy of HSP47. The promote r region contains a TATA box, four Sp1-binding sites and one AP-1-bind ing site. A complete heat-shock element (HSE) was found between nucleo tides (nt) -61 and -79. Furthermore, the heat inducibility was reprodu ced by transfecting mouse BALB/3T3 cells with a plasmid carrying cat u nder the control of the HSE-containing fragment (nt -197 and +38) of H SP47. Computer analysis of the promoter region did not show marked hom ology to other vertebrate promoters.