Isolation and functional analysis of a human 70,000-dalton heat shock protein gene segment (original) (raw)
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Sequence and organization of genes encoding the human 27 kDa heat shock protein
Nucleic Acids Research, 1986
The 27 kDa human heat shock protein (hsp27) is encoded by a gene family of 4 members. Two genomic fragments hybridizing to cDNA encoding hsp27 have been isolated, characterized, and sequenced. One clone is a member of a cluster of three genes linked within a 14-18 kb region of the genome and encodes a transcript interrupted by two intervening sequences. A single open reading frame encodes a polypeptide of 22,300 deduced molecular weight. the 5' flanking region contains two transcription start sites and sequences homologous to the Drosophila consensus heat inducible control element. Induction of both potential transcripts follows heat shock in vivo. Accurate heat inducible transcription occurs at both start sites after injection into Xenopus oocytes. The second genomic clone is a processed pseudogene lacking promoter elements and is unlinked with the other members of the hsp27 gene family. The amino acid sequence of human hsp27 shows striking homology with mammalian a crystallin, and contains a reg ion towards the carboxy terminus which shares homology with the small hsp of rosophila and other organisms.
Gene, 1986
Plasmids containing cDNA copies of mRNAs induced in HeLa cells by heat shock have been isolated and characterized. In vitro translation of RNAs selected by hybridization to plasmid DNAs identified sequences representing the three major classes** (89, 70 and 27-kDa) of heat-shock proteins (hsp) and a 60-kDa minor hsp. Plasmids with inserts specific for the 27, 60, and 70-kDa hsp each hybridize with a single discrete size class of heat-inducible mRNA. Plasmids specific for the 89-kDa protein, however, hybridize with either a 2.7or 2.95kb mRNA species. Both mRNAs are coordinately induced during heat shock. We show that the characteristic pattern of induction and repression of each class of hsp during sustained hyperthermia is the result of changes in the steady state level of each mRNA.
Journal of Biological Chemistry
The two forms of the -90-kDa murine heat shock protein, referred to as HSP86 and HSP84, are coded for by separate but related genes. A full-length nucleotide sequence of the cDNA coding for HSP86 from a chemically induced tumor, Meth A, was determined. Sequences from a number of peptides from HSP86 were found to be in complete agreement with the nucleotide sequence. The HSP84 sequence from the same tumor was also completed. HSP86 and HSP84 are acidic polypeptides 733 and 724 amino acids long with calculated molecular weights of 84,796 and 83,290, respectively. The two proteins are 86% homologous. HSP86 was found to contain internal peptide repeats of Glu-Lys-Glu within a region of highly charged amino acid residues. The coding regions of the cDNAs were 76% homologous; however, this homology did not extend to the 5'-and 3'-untranslated regions. The 5'untranslated region of hsp86 cDNA was considerably longer than that of hsp84 cDNA and, unlike that of hsp84, contained extraneous ATG triplets. Hsp86-related sequences were assigned to chromosomes 12, 11, and 3. An evolutionary tree constructed from HSP9Orelated protein sequences indicated that HSP86 and HSP84 were likely to have diverged more than 500 million years ago. The findings presented herein suggest that HSP86 and HSP84 may have different functions.
Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein
Molecular and cellular biology, 1985
A nearly full-length cDNA clone isolated from the rat pheochromocytoma cell line, PC12, revealed extensive nucleotide sequence similarity between the rat cDNA and the Drosophila melanogaster hsp70 gene. The rat recombinant clone encodes a 71,000-dalton protein that is 70% identical with the dipteran hsp70 protein. Remarkably, a truncated segment of this cDNA clone was originally isolated by immunoreactivity with antisera raised to catecholamine-synthesizing enzymes, suggesting that this heat shock protein and these catecholamine enzymes shared antigenic determinants. The rat hsp70-related mRNA is responsible for the production of a constitutive hsp70 protein, because it is present in abundant amounts in various tissues at normal growth temperatures and is only minimally induced by hyperthermia. The rat hsp70-related sequence is part of a multigene family that extends across species to mice and humans.
Genetic regulation during heat shock and function of heat-shock proteins: a review
Biochemistry and Cell Biology, 1983
The induction by thermal stress of certain specific genes (heat-shock genes) first described in Drosophila has recently been observed in a wide variety of unicellular and multicellular organisms, emphasizing the basic importance of this ubiquitous response. Recent data dealing with the molecular mechanisms involved in the intensive transcriptional and posttranscriptional regulation during heat shock is reviewed with emphasis on the induction of the response and the putative function of the heat-shock proteins. A model showing the various interactions of cellular regulatory mechanisms operating in the heat-shocked cell is presented. While the list of agents or treatments inducing heat-shock proteins (hsp's) in various organisms is increasing, the identification of a hypothetical common inducing factor is elusive. The recently described reorganization of some cytoskeletal elements upon heat shock is discussed both in terms of its potential involvement in transcriptional and (or) t...
Mapping of the gene family for human heat-shock protein 90α to chromosomes 1, 4, 11, and 14
Genomics, 1992
The HSPQO family of heat-shock proteins (encoded by genes for HSPQOa and B) constitutes one of the major groups of proteins that are synthesized at increased rates in response to heat and other forms of stress. We previously isolated two distinct cDNA clones for HSPQOa from human peripheral blood lymphocytes and from HeLa cells transfected with the adenovirus ElA gene, respectively. To determine the organization of this complex multigene family in the human genome, we used three complementary approaches: Southern analysis of a panel of human/hamster somatic cell hybrids, molecular cloning of the cosmid HSPQOa clones from libraries prepared with DNAs from human lymphoblastoid cells, and in situ hybridization to human chromosomes. We demonstrate here that nucleotide sequences that encode HSPSOa map to human chromosomes lq21.2-q22, 4q35, llp14.1-~14.2, and 14q3.2.3. The chromosonml mapping of the loci, ASPCALl, HSPCAL2, HSPCALB, HSPCALI, and the cbaracterization of the respective genes should facilitate clarification of the organization of this gene family and lead to a better understanding of the biological functions of the gene prodUCt .
65 | P a g e HEAT SHOCK PROTEINS -A MINI REVIEW
2020
This article provides an insight towards the various applications of heat shock proteins and also gives a brief introduction, discovery & functions of heat shock proteins. An overview of role of heat shock proteins in cardiovascular disease, infectious diseases & in cancer is discussed. Heat shock proteins, a family of stress inducible proteins are involved in the pathogenesis of atherosclerotic vascular diseases, various infectious disease & also in tumor cells.
Differential expression of heat shock protein (HSP70) mRNAs in rat cells
Experimental cell …, 1996
Heat shock treatment in PC12 cells induces the synthesis of two HSP70 transcripts of 2.55 and 3.05 kb in size, while only a 70-kDa protein is shown by SDS???PAGE. Using reverse transcription???polymerase chain reaction strategy, two mRNA species were amplified from ...
Characterization of HDJ-2, a human 40 kD heat shock protein
The International Journal of Biochemistry & Cell Biology, 1998
Heat shock proteins (HSP) are a large and complex family of proteins that play important roles in cellular function and survival. In previous studies, cDNA for a 45 kD human HSP (HDJ-2) was doned and shown to be homologous to DNA-J, a bacterial HSP [F.