Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84) - PubMed (original) (raw)
Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)
R Shaknovich et al. Mol Cell Biol. 1992 Nov.
Abstract
A murine cardiac lambda gt11 expression library was screened with an amphipathic helix antibody, and a recombinant representing the C-terminal 194 residues of murine HSP90 (HSP84) was cloned. Both recombinant and native HSP90s were then found to rapidly convert a basic helix-loop-helix protein (MyoD1) from an inactive to an active conformation, as assayed by sequence-specific DNA binding. The conversion process involves a transient interaction between HSP90 and MyoD1 and does not result in the formation of a stable tertiary complex. Conversion does not require ATP and occurs stoichiometrically in a dose-dependent fashion. HSP90 is an abundant, ubiquitous, and highly conserved protein present in most eukaryotic cells. These results provide direct evidence that HSP90 can affect the conformational structure of a DNA-binding protein.
Similar articles
- Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90.
Shue G, Kohtz DS. Shue G, et al. J Biol Chem. 1994 Jan 28;269(4):2707-11. J Biol Chem. 1994. PMID: 8300601 - Two adjacent MyoD1-binding sites regulate expression of the acetylcholine receptor alpha-subunit gene.
Piette J, Bessereau JL, Huchet M, Changeux JP. Piette J, et al. Nature. 1990 May 24;345(6273):353-5. doi: 10.1038/345353a0. Nature. 1990. PMID: 2342565 - Two distinct Xenopus genes with homology to MyoD1 are expressed before somite formation in early embryogenesis.
Scales JB, Olson EN, Perry M. Scales JB, et al. Mol Cell Biol. 1990 Apr;10(4):1516-24. doi: 10.1128/mcb.10.4.1516-1524.1990. Mol Cell Biol. 1990. PMID: 1690844 Free PMC article. - DNA binding specificity of the basic-helix-loop-helix protein MASH-1.
Meierhan D, el-Ariss C, Neuenschwander M, Sieber M, Stackhouse JF, Allemann RK. Meierhan D, et al. Biochemistry. 1995 Sep 5;34(35):11026-36. doi: 10.1021/bi00035a008. Biochemistry. 1995. PMID: 7669760
Cited by
- The Hsp90 Molecular Chaperone Regulates the Transcription Factor Network Controlling Chromatin Accessibility.
Gvozdenov Z, Bendix LD, Kolhe J, Freeman BC. Gvozdenov Z, et al. J Mol Biol. 2019 Dec 6;431(24):4993-5003. doi: 10.1016/j.jmb.2019.09.007. Epub 2019 Oct 16. J Mol Biol. 2019. PMID: 31628945 Free PMC article. - Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling.
Genest O, Wickner S, Doyle SM. Genest O, et al. J Biol Chem. 2019 Feb 8;294(6):2109-2120. doi: 10.1074/jbc.REV118.002806. Epub 2018 Nov 6. J Biol Chem. 2019. PMID: 30401745 Free PMC article. Review. - A Chemical Biology Study of Human Pluripotent Stem Cells Unveils HSPA8 as a Key Regulator of Pluripotency.
Geng Y, Zhao Y, Schuster LC, Feng B, Lynn DA, Austin KM, Stoklosa JD, Morrison JD. Geng Y, et al. Stem Cell Reports. 2015 Dec 8;5(6):1143-1154. doi: 10.1016/j.stemcr.2015.09.023. Epub 2015 Nov 5. Stem Cell Reports. 2015. PMID: 26549849 Free PMC article. - IBR5 Modulates Temperature-Dependent, R Protein CHS3-Mediated Defense Responses in Arabidopsis.
Liu J, Yang H, Bao F, Ao K, Zhang X, Zhang Y, Yang S. Liu J, et al. PLoS Genet. 2015 Oct 9;11(10):e1005584. doi: 10.1371/journal.pgen.1005584. eCollection 2015 Oct. PLoS Genet. 2015. PMID: 26451844 Free PMC article. - Four heat shock protein genes of the endoparasitoid wasp, Cotesia vestalis, and their transcriptional profiles in relation to developmental stages and temperature.
Shi M, Wang YN, Zhu N, Chen XX. Shi M, et al. PLoS One. 2013;8(3):e59721. doi: 10.1371/journal.pone.0059721. Epub 2013 Mar 18. PLoS One. 2013. PMID: 23527260 Free PMC article.
References
- Annu Rev Biochem. 1978;47:251-76 - PubMed
- Nature. 1992 Jan 2;355(6355):33-45 - PubMed
- Cell. 1991 Jul 26;66(2):191-7 - PubMed
- J Biol Chem. 1990 Aug 5;265(22):12778-81 - PubMed
- Gene. 1987;56(1):29-40 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous