Activation of human heat shock gene transcription by heat shock, heavy metal ions, and amino acid analogs required the heat shock element (HSE) in the HSP70 promoter. Both heat shock-and metal ion-induced HSP70 gene transcription occurred independently of protein synthesis, whereas induction by amino acid analogs required protein synthesis. We identified a HSE-binding activity from control cells which was easily distinguished by a gel mobility shift assay from the stress-induced HSE-binding activity which appeared following heat shock or chemically induced stress. The kinetics of HSP70 gene transcription paralleled the rapid appearance of stress-induced HSE-binding activity. During recovery from heat shock, both the rate of HSP70 gene transcription and stress-induced HSE-binding activity levels declined and the control HSE-binding activity reappeared. The DNA contacts of the control and stress-induced HSE-binding activities deduced by methylation interference were similar but not identical. While stable complexes with HSE were formed with extracts from both control and stressed cells in vitro at 25°C, only the stress-induced complex was detected when binding reactions were performed at elevated temperatures.

We have examined the posttranscriptional regulation of hsp70 gene expression in two human cell lines, HeLa and 293 cells, which constitutively express high levels of HSP70. HSP70 mRNA translates with high efficiency in both control and heat-shocked cells. Therefore, heat shock is not required for the efficient translation of HSP70 mRNA. Rather, the main effect of heat shock on translation is to suppress the translatability of non-heat shock mRNAs. Heat shock, however, has a marked effect on the stability of HSP70 mRNA; in non-heatshocked cells the half-life of HSP70 mRNA is approximately 50 min, and its stability increases at least 10-fold upon heat shock. Moreover, HSP70 mRNA is more stable in cells treated with protein synthesis inhibitors, suggesting that a heat shock-sensitive labile protein regulates its turnover. An additional effect on posttranscriptional regulation of hsp7O expression can be found in adenovirus-infected cells, in which HSP70 mRNA levels decline precipititously late during infection although hsp7O transcription continues unabated.Expression of the major heat shock protein, HSP70, is under complex regulatory controls exerted at both the transcriptional and translational levels (18,43,55). Transcription of the hsp70 gene is transiently induced by environmental stress such as exposure to heat shock or heavy metals; in human cells the hsp70 gene is also expressed during normal conditions of cell growth at the Gl/S boundary of the cell cycle (49) and in response to serum stimulation (71).The effects of heat shock on posttranscriptional events include the preferential translation of heat shock mRNAs (32,41,42,62). During heat shock, HSP70 mRNA appears to be translated efficiently whereas most preexisting cellular mRNAs (hereafter referred to as "control mRNAs") are poorly translated. The selective translation of heat shock mRNAs is in part due to features within the 5' noncoding region of the mRNA (15,34,46). Although it has been suggested that heat shock mRNAs may require heat shock conditions for their efficient translation (20), there are at least two lines of evidence to suggest that these mRNAs can translate efficiently under non-stress conditions. First, heat shock mRNAs isolated from a variety of organisms translate in extracts prepared from non-heat-shocked wheat germ, Drosophila, rabbit reticulocyte, and other animal cells (for example, see references 5, 32, 37, 39, 47, 56, and 62). Second, heat shock mRNAs are transcribed and translated under a variety of normal conditions of cell growth such as the Gl/S boundary of the cell cycle (49) and during development and differentiation (9, 10, 59; S. S. Banerji, K. L. Laing, and R. I. Morimoto, Genes Devel., in press).Other posttranscriptional events induced by heat shock include a block in pre-mRNA processing (72) and effects on mRNA stability (24). During heat shock, HSP70 mRNA appears to be stable relative to its short half-life in cells recovering from heat shock (22, 23). For example, HSP70 mRNA persists in heat-shocked chicken cells wel...

The consumption of sport events through direct participation can influence participants' perception of happiness with that experiential purchase given the time and resources invested in that experience. The purpose of the study was to examine how sport event service quality aspects operationalized through the physical environment, interaction, and outcome factors influence overall satisfaction with the event and experiential happiness. Data were collected from 300 runners who participated in 5k and 10k races. Structural equation modeling analysis revealed the positive effect of outcome and physical environment factors on satisfaction with the event and the positive influence of event satisfaction and outcome quality on experiential happiness. The overall expectations on the quality of the event experience can be a focus for event managers aiming to achieve social marketing goals related to positive psychology from the event participation.

This paper attempts to examine the relationship between service quality and customer satisfaction in spectator sports. The relationship between these two constructs is examined, first, by a review of the literature to date and, second, by the results of almost 200 questionnaires completed by spectators at two professional basketball games in Athens, Greece. The results of the questionnaire study are examined and, in conclusion, the implications and limitations of the study are discussed. Areas for further research are also suggested.

The nucleotide sequence of the chick beta-actin gene was determined. The gene contains 5 introns; 4 interrupt the translated region at codons 41/42, 120/122, 267, 327/328 and a large intron occurs in the 5' untranslated region. The gene has a 97 nucleotide 5'-untranslated region and a 594 nucleotide 3'-untranslated region. A slight heterogeneity in the position of the poly A addition site exists; polyadenylation can occur at either of two positions two nucleotides apart. The gene codes for an mRNA of 1814 or 1816 nucleotides, excluding the poly(A) tail. In contrast to the chick skeletal muscle actin gene the beta-actin gene lacks the Cys codon between the initiator ATG and the codon for the N-terminal amino acid of the mature protein. In the 5' flanking DNA, 15 nucleotides downstream from the CCAAT sequence, is a tract of 25 nucleotides that is highly homologous to the sequence found in the same region of the rat beta-actin gene.

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