TY - JOUR
T1 - Crowding alters F-actin secondary structure and hydration
AU - Chen, Xiaobing
AU - Roeters, Steven J.
AU - Cavanna, Francis
AU - Alvarado, José
AU - Baiz, Carlos R.
N1 - Funding Information: This work was supported by the National Institutes of Health (R35GM133359) and the Welch Foundation (F-1891). S.J.R. support by the Novo Nordisk Foundation (Facility Grant NanoScat, no. NNF18OC0032628). This research was also supported by the National Science Foundation through the Center for Dynamics and Control of Materials: an NSF MRSEC under Cooperative Agreement No. DMR-1720595. SJR acknowledges support from the Novo Nordisk Foundation (Facility Grant NanoScat, no. NNF18OC0032628) and the Lundbeck Foundation (Postdoc grant R3032018-349). Publisher Copyright: © 2023, Springer Nature Limited.
PY - 2023/12/1
Y1 - 2023/12/1
N2 - Actin, an important component of eukaryotic cell cytoskeleton, regulates cell shape and transport. The morphology and biochemical properties of actin filaments are determined by their structure and protein-protein contacts. Crowded environments can organize filaments into bundles, but less is known about how they affect F-actin structure. This study used 2D IR spectroscopy and spectral calculations to examine how crowding and bundling impact the secondary structure and local environments in filaments and weakly or strongly bundled networks. The results reveal that bundling induces changes in actin’s secondary structure, leading to a decrease in β-sheet and an increase in loop conformations. Strongly bundled networks exhibit a decrease in backbone solvent exposure, with less perturbed α-helices and nearly “locked” β-sheets. Similarly, the loops become less hydrated but maintain a dynamic environment. These findings highlight the role of loop structure in actin network morphology and stability under morphology control by PEG.
AB - Actin, an important component of eukaryotic cell cytoskeleton, regulates cell shape and transport. The morphology and biochemical properties of actin filaments are determined by their structure and protein-protein contacts. Crowded environments can organize filaments into bundles, but less is known about how they affect F-actin structure. This study used 2D IR spectroscopy and spectral calculations to examine how crowding and bundling impact the secondary structure and local environments in filaments and weakly or strongly bundled networks. The results reveal that bundling induces changes in actin’s secondary structure, leading to a decrease in β-sheet and an increase in loop conformations. Strongly bundled networks exhibit a decrease in backbone solvent exposure, with less perturbed α-helices and nearly “locked” β-sheets. Similarly, the loops become less hydrated but maintain a dynamic environment. These findings highlight the role of loop structure in actin network morphology and stability under morphology control by PEG.
UR - http://www.scopus.com/inward/record.url?scp=85169518353&partnerID=8YFLogxK
U2 - https://doi.org/10.1038/s42003-023-05274-3
DO - https://doi.org/10.1038/s42003-023-05274-3
M3 - Article
C2 - 37660224
SN - 2399-3642
VL - 6
JO - Communications Biology
JF - Communications Biology
IS - 1
M1 - 900
ER -