Biochemical Journal
| Autor: | Keane J. Dye, Zhaomin Yang |
|---|---|
| Přispěvatelé: | Biological Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Cyclic di-GMP
Models Molecular Pilus assembly ATPase Allosteric regulation Biochemistry Microbiology Pilus biofilm PilB 03 medical and health sciences chemistry.chemical_compound Allosteric Regulation Bacterial Proteins Protein Domains Adenine nucleotide Molecular Biology Cyclic GMP Research Articles 030304 developmental biology 0303 health sciences biology Molecular Interactions cyclic-di-GMP type IV pili 030306 microbiology Chemistry Effector Cell Biology Cell biology Acidobacteria Adenosine Diphosphate motility biology.protein Enzymology Oxidoreductases Function (biology) Protein Binding |
| Zdroj: | Biochemical Journal |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | PilB is the assembly ATPase for the bacterial type IV pilus (T4P), and as a consequence, it is essential for T4P-mediated bacterial motility. In some cases, PilB has been demonstrated to regulate the production of exopolysaccharide (EPS) during bacterial biofilm development independently of or in addition to its function in pilus assembly. While the ATPase activity of PilB resides at its C-terminal region, the N terminus of a subset of PilBs forms a novel cyclic-di-GMP (cdG)-binding domain. This multi-domain structure suggests that PilB binds cdG and adenine nucleotides through separate domains which may influence the functionality of PilB in both motility and biofilm development. Here, Chloracidobacterium thermophilum PilB is used to investigate ligand binding by its separate domains and by the full-length protein. Our results confirm the specificity of these individual domains for their respective ligands and demonstrate communications between these domains in the full-length protein. It is clear that when the N- and the C-terminal domains of PilB bind to cdG and ADP, respectively, they mutually influence each other in conformation and in their binding to ligands. We propose that the interactions between these domains in response to their ligands play critical roles in modulating or controlling the functions of PilB as a regulator of EPS production and as the T4P assembly ATPase. National Science FoundationNational Science Foundation (NSF) [MCB-1417726, MCB-1919455] This work was supported by National Science Foundation grants MCB-1417726 and MCB-1919455 to Z.Y. |
| Databáze: | OpenAIRE |
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