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Is peptide bond cis/trans isomerization a key stage in the chemo-mechanical cycle of motor proteins?

Biomedical Engineering Department, Technion - Israel Institute of Technology, Haifa, Israel

¹Correspondence: Biomedical Engineering Department, Technion - Israel Institute of Technology, Haifa, 32000, Israel. E-mail: toren{at}tx.technion.ac.il

ABSTRACT

Motor proteins such as myosin and kinesin are responsible for actively directed movement in vivo. The physicochemical mechanism underlying their function is still obscure. A novel and unifying model concerning the motors driving mechanism is suggested here. This model resides within the framework of the well-studied "swinging lever-arm" hypothesis, stating that cis/trans peptide bond isomerization (CTI) is a key stage in the chemo-mechanical coupling within actomyosin—the complex of the motor (myosin) and its specific track (actin). CTI is suggested to propel myosin’s lever-arm swing. The model addresses on the submolecular level a broad spectrum of actomyosin’s functional characteristics, such as kinetics, energetics, force exertion, stepping, and directionality. The model may be tested first with relative ease in kinesin—a smaller motor that could be specifically modified with unnatural amino acids using bacterial expression. Suggested modifications may be used for labeling and functional decoupling.—Tchaicheeyan, O. Is peptide bond cis/trans isomerization a key stage in the chemo-mechanical cycle of motor proteins?

Key Words: energy transduction • kinesin • mechano-chemical coupling • molecular mechanism • myosin