Next Article in Journal
Alteration of Pituitary Tumor Transforming Gene 1 by MicroRNA-186 and 655 Regulates Invasion Ability of Human Oral Squamous Cell Carcinoma
Next Article in Special Issue
Dynamic Assembly/Disassembly of Staphylococcus aureus FtsZ Visualized by High-Speed Atomic Force Microscopy
Previous Article in Journal
Novel Short-Chain Quinones to Treat Vision Loss in a Rat Model of Diabetic Retinopathy
Previous Article in Special Issue
Exploring Large Domain Motions in Proteins Using Atomistic Molecular Dynamics with Enhanced Conformational Sampling
Review

Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights from Escherichia coli UvrD

Biophotonics Laboratory, The Graduate School for the Creation of New Photonics Industries, 1955-1, Kurematsu-cho, Nishi-ku, Hamamatsu, Shizuoka 431-1202, Japan
Int. J. Mol. Sci. 2021, 22(3), 1018; https://doi.org/10.3390/ijms22031018
Received: 23 December 2020 / Revised: 15 January 2021 / Accepted: 18 January 2021 / Published: 20 January 2021
Helicases are nucleic acid-unwinding enzymes that are involved in the maintenance of genome integrity. Several parts of the amino acid sequences of helicases are very similar, and these quite well-conserved amino acid sequences are termed “helicase motifs”. Previous studies by X-ray crystallography and single-molecule measurements have suggested a common underlying mechanism for their function. These studies indicate the role of the helicase motifs in unwinding nucleic acids. In contrast, the sequence and length of the C-terminal amino acids of helicases are highly variable. In this paper, I review past and recent studies that proposed helicase mechanisms and studies that investigated the roles of the C-terminal amino acids on helicase and dimerization activities, primarily on the non-hexermeric Escherichia coli (E. coli) UvrD helicase. Then, I center on my recent study of single-molecule direct visualization of a UvrD mutant lacking the C-terminal 40 amino acids (UvrDΔ40C) used in studies proposing the monomer helicase model. The study demonstrated that multiple UvrDΔ40C molecules jointly participated in DNA unwinding, presumably by forming an oligomer. Thus, the single-molecule observation addressed how the C-terminal amino acids affect the number of helicases bound to DNA, oligomerization, and unwinding activity, which can be applied to other helicases. View Full-Text
Keywords: protein–nucleic acid interactions; helicase; single-molecule fluorescence imaging; C-terminal amino acids; protein assemblies; enzyme function protein–nucleic acid interactions; helicase; single-molecule fluorescence imaging; C-terminal amino acids; protein assemblies; enzyme function
Show Figures

Figure 1

MDPI and ACS Style

Yokota, H. Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights from Escherichia coli UvrD. Int. J. Mol. Sci. 2021, 22, 1018. https://doi.org/10.3390/ijms22031018

AMA Style

Yokota H. Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights from Escherichia coli UvrD. International Journal of Molecular Sciences. 2021; 22(3):1018. https://doi.org/10.3390/ijms22031018

Chicago/Turabian Style

Yokota, Hiroaki. 2021. "Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights from Escherichia coli UvrD" International Journal of Molecular Sciences 22, no. 3: 1018. https://doi.org/10.3390/ijms22031018

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop