The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation

Verfasser / Beitragende:
[Levi McClelland, Sean Seagraves, Md. Khan, Melisa Cherney, Swati Bandi, Justin Culbertson, Bruce Bowler]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/5(2015-07-01), 805-819
Format:
Artikel (online)
ID: 605507767
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024 7 0 |a 10.1007/s00775-015-1267-1  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00775-015-1267-1 
245 0 4 |a The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation  |h [Elektronische Daten]  |c [Levi McClelland, Sean Seagraves, Md. Khan, Melisa Cherney, Swati Bandi, Justin Culbertson, Bruce Bowler] 
520 3 |a Trimethyllysine 72 (tmK72) has been suggested to play a role in sterically constraining the heme crevice dynamics of yeast iso-1-cytochrome c mediated by the Ω-loop D cooperative substructure (residues 70-85). A tmK72A mutation causes a gain in peroxidase activity, a function of cytochrome c that is important early in apoptosis. More than one higher energy state is accessible for the Ω-loop D substructure via tier 0 dynamics. Two of these are alkaline conformers mediated by Lys73 and Lys79. In the current work, the effect of the tmK72A mutation on the thermodynamic and kinetic properties of wild-type iso-1-cytochrome c (yWT versus WT*) and on variants carrying a K73H mutation (yWT/K73H versus WT*/K73H) is studied. Whereas the tmK72A mutation confers increased peroxidase activity in wild-type yeast iso-1-cytochrome c and increased dynamics for formation of a previously studied His79-heme alkaline conformer, the tmK72A mutation speeds return of the His73-heme alkaline conformer to the native state through destabilization of the His73-heme alkaline conformer relative to the native conformer. These opposing behaviors demonstrate that the response of the dynamics of a protein substructure to mutation depends on the nature of the perturbation to the substructure. For a protein substructure which mediates more than one function of a protein through multiple non-native structures, a mutation could change the partitioning between these functions. The current results suggest that the tier 0 dynamics of Ω-loop D that mediates peroxidase activity has similarities to the tier 0 dynamics required to form the His79-heme alkaline conformer. 
540 |a SBIC, 2015 
690 7 |a Cooperative substructure dynamics  |2 nationallicence 
690 7 |a Cytochrome c  |2 nationallicence 
690 7 |a Alkaline conformational transition  |2 nationallicence 
690 7 |a Conformationally gated electron transfer  |2 nationallicence 
690 7 |a Apoptosis  |2 nationallicence 
690 7 |a ET : Electron transfer  |2 nationallicence 
690 7 |a gated ET : Conformationally gated electron transfer  |2 nationallicence 
690 7 |a GdnHCl : Guanidine hydrochloride  |2 nationallicence 
690 7 |a iso-1-Cyt c : Iso-1-cytochrome c  |2 nationallicence 
690 7 |a tmK : Trimethyllysine  |2 nationallicence 
700 1 |a McClelland  |D Levi  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Seagraves  |D Sean  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Khan  |D Md  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Cherney  |D Melisa  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Bandi  |D Swati  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Culbertson  |D Justin  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
700 1 |a Bowler  |D Bruce  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/5(2015-07-01), 805-819  |x 0949-8257  |q 20:5<805  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-015-1267-1  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-015-1267-1  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a McClelland  |D Levi  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Seagraves  |D Sean  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Khan  |D Md  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cherney  |D Melisa  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Bandi  |D Swati  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Culbertson  |D Justin  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Bowler  |D Bruce  |u Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Dynamics, University of Montana, 59812, Missoula, MT, USA  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/5(2015-07-01), 805-819  |x 0949-8257  |q 20:5<805  |1 2015  |2 20  |o 775