Next Article in Journal
AGR2: The Covert Driver and New Dawn of Hepatobiliary and Pancreatic Cancer Treatment
Previous Article in Journal
Lumbrokinase Extracted from Earthworms Synergizes with Bevacizumab and Chemotherapeutics in Treating Non-Small Cell Lung Cancer by Targeted Inactivation of BPTF/VEGF and NF-κB/COX-2 Signaling
Previous Article in Special Issue
Comparison of In-Frame Deletion, Homology-Directed Repair, and Prime Editing-Based Correction of Duchenne Muscular Dystrophy Mutations
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Article

Bifidobacterium bifidum SAM-VI Riboswitch Conformation Change Requires Peripheral Helix Formation

1
College of Biological and Medical Engineering, Donghua University, Shanghai 201620, China
2
National Center for Protein Science Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201204, China
*
Author to whom correspondence should be addressed.
Biomolecules 2024, 14(7), 742; https://doi.org/10.3390/biom14070742
Submission received: 11 May 2024 / Revised: 10 June 2024 / Accepted: 21 June 2024 / Published: 23 June 2024
(This article belongs to the Collection Feature Papers in Biomacromolecules: Nucleic Acids)

Abstract

The Bifidobacterium bifidum SAM-VI riboswitch undergoes dynamic conformational changes that modulate downstream gene expression. Traditional structural methods such as crystallography capture the bound conformation at high resolution, and additional efforts would reveal details from the dynamic transition. Here, we revealed a transcription-dependent conformation model for Bifidobacterium bifidum SAM-VI riboswitch. In this study, we combine small-angle X-ray scattering, chemical probing, and isothermal titration calorimetry to unveil the ligand-binding properties and conformational changes of the Bifidobacterium bifidum SAM-VI riboswitch and its variants. Our results suggest that the SAM-VI riboswitch contains a pre-organized ligand-binding pocket and stabilizes into the bound conformation upon binding to SAM. Whether the P1 stem formed and variations in length critically influence the conformational dynamics of the SAM-VI riboswitch. Our study provides the basis for artificially engineering the riboswitch by manipulating its peripheral sequences without modifying the SAM-binding core.
Keywords: riboswitch; S-adenosyl-methionine; conformational dynamics; SAM-VI riboswitch; 3D modeling; SAXS; SHAPE riboswitch; S-adenosyl-methionine; conformational dynamics; SAM-VI riboswitch; 3D modeling; SAXS; SHAPE

Share and Cite

MDPI and ACS Style

Xiao, W.; Liu, G.; Chen, T.; Zhang, Y.; Lu, C. Bifidobacterium bifidum SAM-VI Riboswitch Conformation Change Requires Peripheral Helix Formation. Biomolecules 2024, 14, 742. https://doi.org/10.3390/biom14070742

AMA Style

Xiao W, Liu G, Chen T, Zhang Y, Lu C. Bifidobacterium bifidum SAM-VI Riboswitch Conformation Change Requires Peripheral Helix Formation. Biomolecules. 2024; 14(7):742. https://doi.org/10.3390/biom14070742

Chicago/Turabian Style

Xiao, Wenwen, Guangfeng Liu, Ting Chen, Yunlong Zhang, and Changrui Lu. 2024. "Bifidobacterium bifidum SAM-VI Riboswitch Conformation Change Requires Peripheral Helix Formation" Biomolecules 14, no. 7: 742. https://doi.org/10.3390/biom14070742

APA Style

Xiao, W., Liu, G., Chen, T., Zhang, Y., & Lu, C. (2024). Bifidobacterium bifidum SAM-VI Riboswitch Conformation Change Requires Peripheral Helix Formation. Biomolecules, 14(7), 742. https://doi.org/10.3390/biom14070742

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

Article Metrics

Back to TopTop