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SlyD Accelerates trans-to-cis Prolyl Isomerization in a Mechanosignaling Protein under Load.
Sengupta, Abhigyan; Rognoni, Lorenz E; Merkel, Ulrich; Zoldák, Gabriel; Rief, Matthias.
Afiliación
  • Sengupta A; Technische Universität München, Physik Department, Center for Functional Protein Assemblies (CPA), Ernst-Otto-Fischer-Str. 8, D-85748 Garching, Germany.
  • Rognoni LE; Technische Universität München, Physik Department, Center for Functional Protein Assemblies (CPA), Ernst-Otto-Fischer-Str. 8, D-85748 Garching, Germany.
  • Merkel U; Technische Universität München, Physik Department, Center for Functional Protein Assemblies (CPA), Ernst-Otto-Fischer-Str. 8, D-85748 Garching, Germany.
  • Zoldák G; Center for Interdisciplinary Biosciences, Technology and Innovation Park, P.J. Safárik University, Trieda SNP 1, 040 11Kosice, Slovakia.
  • Rief M; Technische Universität München, Physik Department, Center for Functional Protein Assemblies (CPA), Ernst-Otto-Fischer-Str. 8, D-85748 Garching, Germany.
J Phys Chem B ; 125(31): 8712-8721, 2021 08 12.
Article en En | MEDLINE | ID: mdl-34279937
Prolyl isomerization is recognized as one of the key regulatory mechanisms, which plays a crucial role in cell signaling, ion channel gating, phage virus infection, and molecular timing. This isomerization is usually slow but often accelerated by an enzyme, called peptidyl-prolyl isomerase (PPIase). In the current project, we investigate using single-molecule force spectroscopy (SMFS) the impact of a bacterial PPIase, SlyD, on the cis-trans isomerization of the proline 2225 (P2225) in an isolated 20th domain of a cytoskeletal mechanosensing protein filamin-A (FlnA20). To explore the FlnA20-PPIase interaction, we have used multiple SMFS modes, like constant velocity, constant distance, and jumping trap experiments. In our previous study, we reported the unique nature of the P2225, which is conserved in all naturally occurring filamins and can slowly (minutes) interconvert between cis-trans isomers, in absence of any PPIase. Our current results show a staggering 25-fold acceleration of the trans-to-cis isomerization rate in the presence of saturating SlyD concentration (7.25 µM) compared to the unenzymatic condition. A SlyD concentration-dependent depletion of the trans isomeric lifetime was also observed. Additionally, we observed that SlyD stabilizes the cis-isomer in the native state of FlnA20 by ∼2 kBT. This is the first single-molecule observation of the cis-trans isomerization catalysis by a PPIase in a mechanosensing protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Isomerasa de Peptidilprolil / Proteínas de Escherichia coli Idioma: En Revista: J Phys Chem B Asunto de la revista: QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Isomerasa de Peptidilprolil / Proteínas de Escherichia coli Idioma: En Revista: J Phys Chem B Asunto de la revista: QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos