The use of the Xenopus oocyte as a model system to analyze the expression and function of eukaryotic heat shock proteins
- PMID: 17459646
- DOI: 10.1016/j.biotechadv.2007.03.003
The use of the Xenopus oocyte as a model system to analyze the expression and function of eukaryotic heat shock proteins
Abstract
The analysis of the expression and function of heat shock protein (hsp) genes, a class of molecular chaperones, has been greatly aided by studies carried out with Xenopus oocytes. The large size of the oocyte facilitates microinjection of DNA, mRNA or protein, permits manual dissection of nuclei, and allows certain assays to be performed with single oocytes. These and other characteristics were useful in identifying the cis- and trans-acting factors involved in hsp gene transcription as well as the role of chaperones and co-chaperones in the repression and activation of heat shock factor. Xenopus oocytes were used to examine heat shock protein (HSP) molecular chaperone function as well as their involvement in intracellular trafficking, maturation, and secretion of protein. Possible new areas of research with this system include the role of membranes in the heat shock response, involvement of HSPs in viral replication and maturation, and in vivo NMR spectroscopy of microinjected HSPs.
Similar articles
-
Analysis of the expression and function of the small heat shock protein gene, hsp27, in Xenopus laevis embryos.Comp Biochem Physiol A Mol Integr Physiol. 2007 May;147(1):112-21. doi: 10.1016/j.cbpa.2006.12.003. Epub 2006 Dec 12. Comp Biochem Physiol A Mol Integr Physiol. 2007. PMID: 17267255
-
Analysis of molecular chaperones using a Xenopus oocyte protein refolding assay.Methods Mol Biol. 2006;322:213-22. doi: 10.1007/978-1-59745-000-3_15. Methods Mol Biol. 2006. PMID: 16739726 Review.
-
Identification of a complex between centrin and heat shock proteins in CSF-arrested Xenopus oocytes and dissociation of the complex following oocyte activation.Dev Biol. 1995 Sep;171(1):51-9. doi: 10.1006/dbio.1995.1259. Dev Biol. 1995. PMID: 7556907
-
Molecular chaperone function of the Rana catesbeiana small heat shock protein, hsp30.Comp Biochem Physiol A Mol Integr Physiol. 2004 Oct;139(2):175-82. doi: 10.1016/j.cbpb.2004.08.006. Comp Biochem Physiol A Mol Integr Physiol. 2004. PMID: 15528166
-
The heat shock response: life on the verge of death.Mol Cell. 2010 Oct 22;40(2):253-66. doi: 10.1016/j.molcel.2010.10.006. Mol Cell. 2010. PMID: 20965420 Review.
Cited by
-
The Zahn drawings: new illustrations of Xenopus embryo and tadpole stages for studies of craniofacial development.Development. 2017 Aug 1;144(15):2708-2713. doi: 10.1242/dev.151308. Development. 2017. PMID: 28765211 Free PMC article.
-
Adverse effects of fly ashes used as immobilizing agents for highly metal-contaminated soils on Xenopus laevis oocytes survival and maturation-a study performed in the north of France with field soil extracts.Environ Sci Pollut Res Int. 2020 Feb;27(4):3706-3714. doi: 10.1007/s11356-019-04560-0. Epub 2019 Mar 14. Environ Sci Pollut Res Int. 2020. PMID: 30875069
-
Effects of Ferrocenyl 4-(Imino)-1,4-Dihydro-quinolines on Xenopus laevis Prophase I - Arrested Oocytes: Survival and Hormonal-Induced M-Phase Entry.Int J Mol Sci. 2020 Apr 26;21(9):3049. doi: 10.3390/ijms21093049. Int J Mol Sci. 2020. PMID: 32357477 Free PMC article.
-
Putative cis-regulatory elements associated with heat shock genes activated during excystation of Cryptosporidium parvum.PLoS One. 2010 Mar 4;5(3):e9512. doi: 10.1371/journal.pone.0009512. PLoS One. 2010. PMID: 20209102 Free PMC article.
-
Proproliferative functions of Drosophila small mitochondrial heat shock protein 22 in human cells.J Biol Chem. 2010 Feb 5;285(6):3833-3839. doi: 10.1074/jbc.M109.080424. Epub 2009 Nov 30. J Biol Chem. 2010. PMID: 19948727 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources