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DC Field | Value | Language |
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dc.contributor.author | Arora, Kanika | - |
dc.contributor.author | Thakur, Bhishem | - |
dc.contributor.author | Mrigwani, Arpita | - |
dc.contributor.author | Guptasarma, Purnananda | - |
dc.date.accessioned | 2023-08-09T18:59:12Z | - |
dc.date.available | 2023-08-09T18:59:12Z | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | Biochemistry, 60(23), 1836–1852. | en_US |
dc.identifier.uri | https://doi.org/10.1021/acs.biochem.1c00081 | - |
dc.identifier.uri | http://hdl.handle.net/123456789/4438 | - |
dc.description | Only IISER Mohali authors are available in the record. | en_US |
dc.description.abstract | HU is a bacterial nucleoid-associated protein. Two homologues, known as HU-A, and HU-B, are found in Escherichia coli within which the early, late, and stationary phases of growth are dominated by HU-AA, HU-BB, and HU-AB dimers, respectively. Here, using genetic manipulation, mass spectrometry, spectroscopy, chromatography, and electrophoretic examination of glutaraldehyde-mediated cross-linking of subunits, in combination with experiments involving mixing, co-expression, unfolding, and refolding of HU chains, we show that the spontaneous formation of HU-AB heterodimers that is reported to occur upon mixing of wild-type HU-AA and HU-BB homodimers does not occur if chains possess N-terminal extensions. We show that N-terminal extensions interfere with the conversion of homodimers into heterodimers. We also show that heterodimers are readily formed at anticipated levels by chains possessing N-terminal extensions in vivo, when direct chain–chain interactions are facilitated through production of HU-A and HU-B chains from proximal genes located upon the same plasmid. From the data, two explanations emerge regarding the mechanism by which N-terminal extensions happen to adversely affect the conversion of homodimers into heterodimers. (1) The disappearance of the α-amino group at HU’s N-terminus impacts the intersubunit stacking of β-sheets at HU’s dimeric interface, reducing the ease with which subunits dissociate from each other. Simultaneously, (2) the presence of an N-terminal extension appears to sterically prevent the association of HU-AA and HU-BB homodimers into a critically required, heterotetrameric intermediate (within which homodimers could otherwise exchange subunits without releasing monomers into solution, by remaining physically associated with each other). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | ACS Publication | en_US |
dc.subject | HU Heterodimer | en_US |
dc.subject | Strengthening Intersubunit | en_US |
dc.subject | Heterotetrameric | en_US |
dc.subject | N-Terminal | en_US |
dc.title | N-Terminal Extensions Appear to Frustrate HU Heterodimer Formation by Strengthening Intersubunit Contacts and Blocking the Formation of a Heterotetrameric Intermediate | en_US |
dc.type | Article | en_US |
Appears in Collections: | Research Articles |
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Need To Add…Full Text_PDF..pdf | Only IISER Mohali authors are available in the record. | 15.36 kB | Adobe PDF | View/Open |
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