D-Loop Mutation G42A/G46A Decreases Actin Dynamics
| Autor: | Masahito Hayashi, Tomoharu Matsumoto, Yuichiro Maéda, Ikuko Fujiwara, Akihiro Narita, Toshiro Oda, Kayo Maeda, Sae Kashima, Mizuki Matsuzaki, Kingo Takiguchi |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular lcsh:QR1-502 cofilin macromolecular substances intrinsically disordered medicine.disease_cause Biochemistry lcsh:Microbiology Article Protein Structure Secondary Polymerization Protein filament 03 medical and health sciences 0302 clinical medicine medicine Humans depolymerization Amino Acid Sequence Cytoskeleton Beta (finance) Molecular Biology Actin 030304 developmental biology 0303 health sciences Mutation Chemistry Depolymerization Cofilin Actins Recombinant Proteins Actin Cytoskeleton Protein Subunits Actin Depolymerizing Factors Biophysics 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Biomolecules Biomolecules, Vol 10, Iss 736, p 736 (2020) Volume 10 Issue 5 |
| ISSN: | 2218-273X |
| DOI: | 10.3390/biom10050736 |
| Popis: | Depolymerization and polymerization of the actin filament are indispensable in eukaryotes. The DNase I binding loop (D-loop), which forms part of the interface between the subunits in the actin filament, is an intrinsically disordered loop with a large degree of conformational freedom. Introduction of the double mutation G42A/G46A to the D-loop of the beta cytoskeletal mammalian actin restricted D-loop conformational freedom, whereas changes to the critical concentration were not large, and no major structural changes were observed. Polymerization and depolymerization rates at both ends of the filament were reduced, and cofilin binding was inhibited by the double mutation. These results indicate that the two glycines at the tip of the D-loop are important for actin dynamics, most likely by contributing to the large degree of conformational freedom. |
| Databáze: | OpenAIRE |
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