Abstract

To gain insight into the mechanisms of gene control, I propose to study the genes related to the major Drosophila heat shock protein of both Drosophila and the bacterium E. coli. The response of organims to heat and other stresses is universal and the proteins induced by treatment have been conserved throughout evolution. We have found a family of genes related to the major heat shcok inducible gene of Drosophila. A number of these genes are transcribed at normal growth temperature and not induced by heat shock. Also we have identified a gene in E. coli which is related to the Drosophila hsp 70 gene and whose transcription is enhanced by heat treatment. The approach to study the regulation and function of these genes will be three-fold. First, we will analyze the transcription of these hsp 70 related genes of Drosophila in different tissues and developmental stages. Secondly, a genetic analysis will be carried out on the 87D Drosophila gene and the E. coli gene to gain insight into the function of these genes. Thirdly, monoclonal antibodies specific for the various protein products will be used to determine the location of these proteins in normal and mutant cells, under normal and heat shock conditions, in order to gain insight into the function of these related proteins. Also, transcription and genetic analysis will be carried out on the 87E actin gene to gain insight into the function and interation of the multigene family of actin genes.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM027870-06
Application #
3275082
Study Section
Genetics Study Section (GEN)
Project Start
1980-04-01
Project End
1988-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
6
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Wisconsin Madison
Department
Type
Schools of Medicine
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715

  Publications

Craig, Elizabeth A (2018) Hsp70 at the membrane: driving protein translocation. BMC Biol 16:11
Schilke, Brenda A; Ciesielski, Szymon J; Ziegelhoffer, Thomas et al. (2017) Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. PLoS Genet 13:e1007084
Dutkiewicz, Rafal; Nowak, Malgorzata; Craig, Elizabeth A et al. (2017) Fe-S Cluster Hsp70 Chaperones: The ATPase Cycle and Protein Interactions. Methods Enzymol 595:161-184
Ciesielski, Szymon J; Craig, Elizabeth A (2017) Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism. Curr Genet 63:51-56
Craig, Elizabeth A; Marszalek, Jaroslaw (2017) How Do J-Proteins Get Hsp70 to Do So Many Different Things? Trends Biochem Sci 42:355-368
Lee, Kanghyun; Sharma, Ruchika; Shrestha, Om Kumar et al. (2016) Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits. Nat Struct Mol Biol 23:1003-1010
Delewski, Wojciech; Paterkiewicz, Bogumi?a; Manicki, Mateusz et al. (2016) Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein Interaction. Mol Biol Evol 33:643-56
Ciesielski, Szymon J; Schilke, Brenda; Marszalek, Jaroslaw et al. (2016) Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation. Mol Biol Cell 27:1060-8
Schmitz-Abe, Klaus; Ciesielski, Szymon J; Schmidt, Paul J et al. (2015) Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9. Blood 126:2734-8
Yu, Hyun Young; Ziegelhoffer, Thomas; Craig, Elizabeth A (2015) Functionality of Class A and Class B J-protein co-chaperones with Hsp70. FEBS Lett 589:2825-30

Showing the most recent 10 out of 51 publications