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Enhancing the population of the encounter complex affects protein complex formation efficiency

Title data

Di Savino, Antonella ; Förster, Johannes ; Ullmann, G. Matthias ; Ubbink, Marcellus:
Enhancing the population of the encounter complex affects protein complex formation efficiency.
In: The FEBS Journal. (17 August 2021) .
ISSN 1742-4658
DOI: https://doi.org/10.1111/febs.16159

Official URL: Volltext

Project information

Project title:
Project's official titleProject's id
SFB 1357 MikroplastikSFB1357

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

Optimal charge distribution is considered to be important for efficient formation of protein complexes. Electrostatic interactions guide encounter complex formation that precedes the formation of an active protein complex. However, disturbing the optimized distribution by introduction of extra charged patches on cytochrome c peroxidase does not lead to a reduction in productive encounters with its partner cytochrome c. To test whether a complex with a high population of encounter complex is more easily affected by suboptimal charge distribution, the interactions of cytochrome c mutant R13A with wild type cytochrome c peroxidase and a variant with an additional negative patch were studied. The complex of the peroxidase and cytochrome c R13A was reported to have an encounter state population of 80%, compared to 30% for the wild type cytochrome c. NMR analysis confirms the dynamic nature of the interaction and demonstrates that the mutant cytochrome c samples the introduced negative patch. Kinetic experiments show that productive complex formation is 5-7 fold slower at moderate and high ionic strength values for cytochrome c R13A but the association rate is not affected by the additional negative patch on cytochrome c peroxidase, showing that the total charge on the protein surface can compensate for less optimal charge distribution. At low ionic strength (44 mM), the association with the mutant cytochrome c reaches the same high rates as found for wild type cytochrome c, approaching the diffusion limit.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: protein-protein interactions; encounter complex; electrostatic interactions
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professor Bioinformatics/Structural Biology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professor Bioinformatics/Structural Biology > Professor Bioinformatics/Structural Biology - Univ.-Prof. Dr. Matthias Ullmann
Research Institutions > Collaborative Research Centers, Research Unit > SFB 1357 - MIKROPLASTIK
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 530 Physics
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 25 Aug 2021 09:26
Last Modified: 25 Aug 2021 09:26
URI: https://eref.uni-bayreuth.de/id/eprint/66835