Emeritus Group Prof. Ernst Bamberg

Emeritus Group Prof. Ernst Bamberg

 

Functional analysis of electrogenic membrane proteins

The focus of the research the emeritus group is the functional analysis of electrogenic membrane proteins. Transporters, ion pumps as well as ion channels are under investigation. Electrical, electrophysiological and spectroscopic methods are applied.

The methodological spectrum is completed by protein purification and molecular biology approaches In order to obtain a detailed view of the transport across the membrane kinetic methods are applied to study transport and conformational dynamics of the proteins in situ and in vitro. The main topic is the functional and structural analysis of microbial rhodopsins, which can be used as optogenetic tools. The most prominent player within this class of proteins is channelrhodopsin 2 (ChR2). ChR2 was described by us as the first light-gated channel, which became a long sought tool in neurobiology, because its insertion in electrically excitable cells(neurons, muscle cells) yields the depolarization thereby the activation of the cells.

Expression of ChR2 together with light-activated rhodopsin like hyperpolarizing ion pumps, allows the multimodal control of the cells in culture as well as in living animals simply by light with high spatiotemporal resolution in a minimally invasive manner. ChR2 and our newly developed analogues are used worldwide for basic neurobiological research, for biomedical applications and for drug discovery as well.


Recent Publications

1.
Bratanov, D., Kovalev, K., Machtens, J.-P., Astashkin, R., Chizhov, I., Soloviov, D., Volkov, D., Polovinkin, V., Zabelskii, D., Mager, T., Gushchin, I., Rokitskaya, T., Antonenko, Y., Alekseev, A., Shevchenko, V., Yutin, N., Rosselli, R., Baeken, C., Borshchevskiy, V., Bourenkov, G., Popov, A., Balandin, T., Büldt, G., Manstein, D. J., Rodriguez-Valera, F., Fahlke, C., Bamberg, E., Koonin, E., and Gordeliy, V.
Unique structure and function of viral rhodopsins.
Nature Communications, 10(1), 4939. (2019). https://dx.doi.org/10.1038/s41467-019-12718-0
2.
Ehrenberg, D., Krause, N., Saita, M., Bamann, C., Kar, R.K., Hoffmann, K., Heinrich, D., Schapiro, I., Heberle, J., and Schlesinger, R.
Atomistic Insight into the Role of Threonine 127 in the Functional Mechanism of Channelrhodopsin-2.
Applied Sciences 9, (22), 4905, (2019). https://dx.doi.org/10.3390/app9224905
3.
Henderson, R.K., Fendler, K. and Poolman, B.
Coupling efficiency of secondary active transporters.
Curr. Opin. Biotechnol. 58, 62-71 (2019). https://dx.doi.org/10.1016/j.copbio.2018.11.005
4.
Kaur, J., Kriebel, C.N., Eberhardt, P., Jakdetchai, O., Leeder, A.J., Weber, I., Brown, L.J., Brown, R.C.D., Becker-Baldus, J., Bamann, C., Wachtveitl, J. and Glaubitz, C.
Solid-state NMR analysis of the sodium pump Krokinobacter rhodopsin 2 and its H30A mutant.
J Struct Biol. 206 (1) 55-65 (2019) https://dx.doi.org/10.1016/j.jsb.2018.06.001
5.
Kovalev, K., Polovinkin, V., Gushchin, I., Alekseev, A., Shevchenko, V., Borshchevskiy, V., Astashkin, R., Balandin, T., Bratanov, D., Vaganova, S., Popov, A., Chupin, V., Buldt, G., Bamberg, E., and Gordeliy, V.
Structure and mechanisms of sodium-pumping KR2 rhodopsin.
Sci Adv, 5(4), eaav2671. (2019) https://dx.doi.org/10.1126/sciadv.aav2671
6.
Mikušević, V., Schrecker, M., Kolesova, N., Patiño-Ruiz, M., Fendler, K., and Hänelt, I.
A channel profile report of the unusual K+ channel KtrB.
The Journal of General Physiology, jgp.201912384. (2019). https://dx.doi.org/10.1085/jgp.201912384
7.
Patiño-Ruiz, M., Fendler, K., and Călinescu, O.
Mutation of two key aspartate residues alters stoichiometry of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
Scientific Reports, 9(1), 15390. (2019) https://dx.doi.org/10.1038/s41598-019-51887-2
8.
Patiño-Ruiz, M., Dwivedi, M., Călinescu, O., Karabel, M., Padan, E., and Fendler, K.
Replacement of Lys-300 with a glutamine in the NhaA Na+/H+ antiporter of Escherichia coli yields a functional electrogenic transporter.
Journal of Biological Chemistry, 294 (1), 246-256. (2019) https://dx.doi.org/10.1074/jbc.RA118.004903

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