Article ; Online: Dynamic cycling with a unique Hsp90/Hsp70-dependent chaperone machinery and GAPDH is needed for heme insertion and activation of neuronal NO synthase.
The Journal of biological chemistry
2022 Volume 299, Issue 2, Page(s) 102856
Abstract: Heat shock protein 90 (Hsp90) is known to mediate heme insertion and activation of heme-deficient neuronal nitric oxide (NO) synthase (apo-nNOS) in cells by a highly dynamic interaction that has been extremely difficult to study mechanistically with the ... ...
Abstract | Heat shock protein 90 (Hsp90) is known to mediate heme insertion and activation of heme-deficient neuronal nitric oxide (NO) synthase (apo-nNOS) in cells by a highly dynamic interaction that has been extremely difficult to study mechanistically with the use of subcellular systems. In that the heme content of many critical hemeproteins is regulated by Hsp90 and the heme chaperone GAPDH, the development of an in vitro system for the study of this chaperone-mediated heme regulation would be extremely useful. Here, we show that use of an antibody-immobilized apo-nNOS led not only to successful assembly of chaperone complexes but the ability to show a clear dependence on Hsp90 and GAPDH for heme-mediated activation of apo-nNOS. The kinetics of binding for Hsp70 and Hsp90, the ATP and K |
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MeSH term(s) | Heme/chemistry ; Hemeproteins/chemistry ; Hemeproteins/metabolism ; HSP70 Heat-Shock Proteins/chemistry ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/chemistry ; HSP90 Heat-Shock Proteins/metabolism ; Molecular Chaperones/chemistry ; Molecular Chaperones/metabolism ; Protein Binding ; Nitric Oxide Synthase/chemistry ; Nitric Oxide Synthase/metabolism ; Enzymes, Immobilized ; Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; Enzyme Activation |
Chemical Substances | Heme (42VZT0U6YR) ; Hemeproteins ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Molecular Chaperones ; Nitric Oxide Synthase (EC 1.14.13.39) ; Enzymes, Immobilized ; Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-) |
Language | English |
Publishing date | 2022-12-31 |
Publishing country | United States |
Document type | Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't |
ZDB-ID | 2997-x |
ISSN | 1083-351X ; 0021-9258 |
ISSN (online) | 1083-351X |
ISSN | 0021-9258 |
DOI | 10.1016/j.jbc.2022.102856 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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