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Characterization and expression of the mouse Hsc70 gene
C R Hunt1, A J Parsian, P C Goswami
1Washington University School of Medicine, Radiation Oncology Center, 4511 Forest Park Blvd., St. Louis, MO 63108, USA. hunt@radonc.wustl.edu
Biochimica Et Biophysica Acta
|March 30, 1999
Summary
The mouse Hsc70 gene, located on Chr 9, shows universal expression, with levels varying by tissue. Hsc70 (Heat Shock Chaperone 70) mRNA is inducible by stress and cell cycle, suggesting roles in protein homeostasis.
Area of Science:
- Molecular Biology
- Genetics
- Cell Biology
Background:
- Heat Shock Chaperone 70 (Hsc70) is a crucial protein involved in cellular homeostasis.
- Understanding the regulation of Hsc70 gene expression is vital for comprehending cellular stress responses and protein quality control.
Purpose of the Study:
- To isolate and characterize the mouse Hsc70 gene.
- To investigate the regulation of Hsc70 gene expression in response to cellular stress and cell cycle progression.
Main Methods:
- Genomic DNA isolation and sequencing.
- Genetic mapping to determine gene location.
- Quantitative analysis of Hsc70 mRNA levels in various tissues and cell lines.
- Treatment of cultured cells with azetidine and MG132 to induce Hsc70 expression.
- Cell cycle analysis to assess Hsc70 expression patterns.
Main Results:
- The mouse Hsc70 gene is approximately 3.9 kb and contains eight introns, with three encoding U14 snoRNAs.
- The Hsc70 gene is mapped to Chr 9.
- Hsc70 expression is widespread in mouse tissues, with notable variations.
- Hsc70 mRNA levels are significantly induced in NIH 3T3 and HeLa cells by azetidine and MG132.
- Human Hsc70 gene expression is cell-cycle regulated, peaking in late G1/S-phase.
Conclusions:
- The mouse Hsc70 gene structure and chromosomal location have been elucidated.
- Hsc70 expression is dynamically regulated by cellular stress and cell cycle, indicating its involvement in protein degradation and cellular stress response pathways.
- The findings provide insights into the complex regulatory mechanisms governing Hsc70 expression in mammals.