Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The nutrient germinant receptors (GRs) in spores of Bacillus species consist of a cluster of three proteins- designated A, B, and C subunits- that play a critical role in initiating the germination of dormant spores in response to specific nutrient molecules. The Bacillus cereus GerI GR is essential for inosine-induced germination; however, the roles of the individual subunits and the mechanism by which germinant binding activates GR function remain unclear. In this study, we report the backbone chemical shift assignments of the N-terminal domain (NTD) of the A subunit of GerI (GerIA). Furthermore, we derive the secondary structure of GerIA in solution and compare it with the crystal structure of the NTD of the A subunit of a Bacillus megaterium GR. These findings lay the foundation for further NMR studies aimed at investigating the structure-function relationship of the GerI subunits, with a broader goal of understanding the molecular mechanism underlying germinant recognition and signal transduction in GRs across Bacillus species.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s12104-025-10216-7 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration.
Curr Biol
September 2025
Department of Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616, USA. Electronic address:
Nuclear migration plays a fundamental role in development, requiring precise spatiotemporal control of bidirectional movement through dynein and kinesin motors. Here, we uncover a differential isoform-dependent mechanism for developmental regulation of nuclear migration directionality. The nuclear envelope Klarsicht/ANC-1/Syne homology (KASH) protein UNC-83 in Caenorhabditis elegans exists in multiple isoforms that differentially control motor activity to achieve tissue-specific nuclear positioning.
View Article and Find Full Text PDFDiscovery and phylogeny of a ricin-B-like domain from rice.
Carbohydr Res
September 2025
Laboratory for Biochemistry & Glycobiology, Ghent University, Department of Biotechnology, Ghent, Belgium. Electronic address:
Lectins are carbohydrate-binding proteins which play key roles in various biological processes, including cell signaling, pathogen recognition and development. Previous research conducted on ricin-B lectin domains and carbohydrate-binding modules of family 13 (CBM13) illustrated the striking resemblances between these two groups of protein domains. In this study, we report on the discovery, identification and putative biochemical characteristics of a ricin-B-like domain that is unique for GH27 enzymes from land plants, identified in the OsAPSE enzyme from Japanese rice (Oryza sativa L.
View Article and Find Full Text PDFIntrinsically disordered region of Clr4/Suv39 regulates its enzymatic activity and ensures heterochromatin spreading.
Nucleic Acids Res
September 2025
Division of Chromatin Regulation, National Institute for Basic Biology, Okazaki 444-8585, Japan.
Methylation of histone H3 at lysine 9 (H3K9me), a hallmark of heterochromatin, is catalyzed by Clr4/Suv39. Clr4/Suv39 contains two conserved domains-an N-terminal chromodomain and a C-terminal catalytic domain-connected by an intrinsically disordered region (IDR). Several mechanisms have been proposed to regulate Clr4/Suv39 activity, but how it is regulated under physiological conditions remains largely unknown.
View Article and Find Full Text PDFMoss BRCA2 lacking the canonical DNA-binding domain promotes homologous recombination and binds to DNA.
Nucleic Acids Res
September 2025
Université Paris-Saclay, INRAE, AgroParisTech, Institut Jean-Pierre Bourgin for Plant Sciences (IJPB), 78000 Versailles, France.
BRCA2 is crucial for mediating homology-directed DNA repair (HDR) through its binding to single-stranded DNA (ssDNA) and the recombinases RAD51 and DMC1. Most BRCA2 orthologs have a canonical DNA-binding domain (DBD) with the exception of Drosophila melanogaster. It remains unclear whether such a noncanonical BRCA2 variant without DBD possesses a DNA-binding activity.
View Article and Find Full Text PDFGastrointestinal stability and DPP-IV inhibitory activity of tilapia (Oreochromis niloticus) viscera hydrolysate-derived novel peptides LPCL and TPFLPDE, with LPCL-modulated GLP-1 and PepT1 expression in STC-1 cells.
Food Res Int
November 2025
Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung 811, Taiwan. Electronic address:
Dipeptidyl-peptidase (DPP)-IV inhibition by penultimate N-terminus Pro-containing peptides is a promising strategy for Type 2 diabetes (T2D) management, as it prevents the degradation of incretin hormones (DPP-IV substrates) like glucagon-like peptide-1 (GLP-1), thereby prolonging their half-life. However, the stability and bio-accessibility of these peptides are crucial to their efficacy in orally administered therapeutics. We previously identified LPCL and TPFLPDE peptides from tilapia viscera by-products hydrolysates, which exhibited significant DPP-IV inhibition in vitro and in situ while effectively preserving active GLP-1 levels after 2 h treatment in STC-1 cells under basal glucose conditions.
View Article and Find Full Text PDF