When a foreign gene meets its native counterpart : computational biophysics analysis of two PgiC loci in the grass Festuca ovina
(2020) In Scientific Reports 10(1).- Abstract
Duplicative horizontal gene transfer may bring two previously separated homologous genes together, which may raise questions about the interplay between the gene products. One such gene pair is the “native” PgiC1 and “foreign” PgiC2 in the perennial grass Festuca ovina. Both PgiC1 and PgiC2 encode cytosolic phosphoglucose isomerase, a dimeric enzyme whose proper binding is functionally essential. Here, we use biophysical simulations to explore the inter-monomer binding of the two homodimers and the heterodimer that can be produced by PgiC1 and PgiC2 in F. ovina. Using simulated native-state ensembles, we examine the structural properties and binding tightness of the dimers. In addition, we investigate their ability to withstand... (More)
Duplicative horizontal gene transfer may bring two previously separated homologous genes together, which may raise questions about the interplay between the gene products. One such gene pair is the “native” PgiC1 and “foreign” PgiC2 in the perennial grass Festuca ovina. Both PgiC1 and PgiC2 encode cytosolic phosphoglucose isomerase, a dimeric enzyme whose proper binding is functionally essential. Here, we use biophysical simulations to explore the inter-monomer binding of the two homodimers and the heterodimer that can be produced by PgiC1 and PgiC2 in F. ovina. Using simulated native-state ensembles, we examine the structural properties and binding tightness of the dimers. In addition, we investigate their ability to withstand dissociation when pulled by a force. Our results suggest that the inter-monomer binding is tighter in the PgiC2 than the PgiC1 homodimer, which could explain the more frequent occurrence of the foreign PgiC2 homodimer in dry habitats. We further find that the PgiC1 and PgiC2 monomers are compatible with heterodimer formation; the computed binding tightness is comparable to that of the PgiC1 homodimer. Enhanced homodimer stability and capability of heterodimer formation with PgiC1 are properties of PgiC2 that may contribute to the retaining of the otherwise redundant PgiC2 gene.
(Less)
- author
- Li, Yuan
LU
; Mohanty, Sandipan
LU
; Nilsson, Daniel
LU
; Hansson, Bengt
LU
; Mao, Kangshan and Irbäck, Anders LU
- organization
-
- Computational Biology and Biological Physics - Has been reorganised
- ELLIIT: the Linköping-Lund initiative on IT and mobile communication
- eSSENCE: The e-Science Collaboration
- Molecular Ecology and Evolution Lab (research group)
- MEMEG
- Genetics of Sex Differences (research group)
- Computational Science for Health and Environment (research group)
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scientific Reports
- volume
- 10
- issue
- 1
- article number
- 18752
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:33127989
- scopus:85094669426
- ISSN
- 2045-2322
- DOI
- 10.1038/s41598-020-75650-0
- language
- English
- LU publication?
- yes
- id
- 09b13561-0686-4bac-8707-9dc0fe7ddc4c
- date added to LUP
- 2020-11-13 08:38:45
- date last changed
- 2025-01-10 23:12:52
@article{09b13561-0686-4bac-8707-9dc0fe7ddc4c, abstract = {{<p>Duplicative horizontal gene transfer may bring two previously separated homologous genes together, which may raise questions about the interplay between the gene products. One such gene pair is the “native” PgiC1 and “foreign” PgiC2 in the perennial grass Festuca ovina. Both PgiC1 and PgiC2 encode cytosolic phosphoglucose isomerase, a dimeric enzyme whose proper binding is functionally essential. Here, we use biophysical simulations to explore the inter-monomer binding of the two homodimers and the heterodimer that can be produced by PgiC1 and PgiC2 in F. ovina. Using simulated native-state ensembles, we examine the structural properties and binding tightness of the dimers. In addition, we investigate their ability to withstand dissociation when pulled by a force. Our results suggest that the inter-monomer binding is tighter in the PgiC2 than the PgiC1 homodimer, which could explain the more frequent occurrence of the foreign PgiC2 homodimer in dry habitats. We further find that the PgiC1 and PgiC2 monomers are compatible with heterodimer formation; the computed binding tightness is comparable to that of the PgiC1 homodimer. Enhanced homodimer stability and capability of heterodimer formation with PgiC1 are properties of PgiC2 that may contribute to the retaining of the otherwise redundant PgiC2 gene.</p>}}, author = {{Li, Yuan and Mohanty, Sandipan and Nilsson, Daniel and Hansson, Bengt and Mao, Kangshan and Irbäck, Anders}}, issn = {{2045-2322}}, language = {{eng}}, number = {{1}}, publisher = {{Nature Publishing Group}}, series = {{Scientific Reports}}, title = {{When a foreign gene meets its native counterpart : computational biophysics analysis of two PgiC loci in the grass Festuca ovina}}, url = {{http://dx.doi.org/10.1038/s41598-020-75650-0}}, doi = {{10.1038/s41598-020-75650-0}}, volume = {{10}}, year = {{2020}}, }