Abstract
The eukaryotic genome encodes a large multigene family of proteins that share extensive sequence identity and biochemical properties with the major heat shock-inducible protein, HSP70. In human cells there are at least five distinct members of the HSP70 gene family that are constitutively expressed or induced in response to physiological stress. The genes that encode many of these HSP70-related proteins have been cloned, and comparison of their corresponding nucleotide sequences has revealed a high degree of evolutionary conservation among members of the HSP70 family within a single species and between species (Moran et al. 1982; Lowe et al. 1983; Hunt and Morimoto 1985; Mues et al. 1986). For example, comparison of heat shock proteins between species as separated as dnaK from E. coli and human HSP70 reveals 50% identity at the amino acid level (Bardwell and Craig 1984). Among the human HSP70-related proteins, GRP78 and HSP70 are 76% identical while P72 and HSP70 are 85% identical (Hunt and Morimoto 1985).
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© 1990 Springer-Verlag Berlin Heidelberg
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Morimoto, R.I., Abravaya, K., Mosser, D., Williams, G.T. (1990). Transcription of the Human HSP70 Gene: cis-Acting Elements and trans-Acting Factors Involved in Basal, Adenovirus E1A, and Stress-Induced Expression. In: Schlesinger, M.J., Santoro, M.G., Garaci, E. (eds) Stress Proteins. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75815-7_1
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DOI: https://doi.org/10.1007/978-3-642-75815-7_1
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