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Domain-specific cha...
Domain-specific chaperone-induced expansion is required for ß-actin folding : a comparison of ß-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC)
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- Villebeck, Laila (författare)
- Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan
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- Moparthi, Satish Babu (författare)
- Linköpings universitet,Institutionen för fysik, kemi och biologi,Tekniska högskolan
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- Lindgren, Mikael (författare)
- Department of Physics, Norwegian University of Science and Technology, 7491 Trondheim, Norway
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- Hammarström, Per (författare)
- Linköpings universitet,Institutionen för fysik, kemi och biologi,Tekniska högskolan
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- Jonsson, Bengt-Harald (författare)
- Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan
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(creator_code:org_t)
- 2007-10-16
- 2007
- Engelska.
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 46:44, s. 12639-12647
- Relaterad länk:
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http://urn.kb.se/res...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Actin, an abundant cytosolic protein in eukaryotic cells, is dependent on the interaction with the chaperonin tail-less complex polypeptide 1 ring complex (TRiC) to fold to the native state. The prokaryotic chaperonin GroEL also binds non-native ß-actin, but is unable to guide ß-actin toward the native state. In this study we identify conformational rearrangements in ß-actin, by observing similarities and differences in the action of the two chaperonins. A cooperative collapse of ß-actin from the denatured state to an aggregation-prone intermediate is observed, and insoluble aggregates are formed in the absence of chaperonin. In the presence of GroEL, however, >90% of the aggregation-prone actin intermediate is kept in solution, which shows that the binding of non-native actin to GroEL is effective. The action of GroEL on bound flourescein-labeled ß-actin was characterized, and the structural rearrangement was compared to the case of the ß-actin-TRiC complex, employing the homo fluorescence resonance energy transfer methodology previously used [Villebeck, L., Persson, M., Luan, S.-L., Hammarström, P., Lindgren, M., and Jonsson, B.-H. (2007) Biochemistry 46 (17), 5083-93]. The results suggest that the actin structure is rearranged by a "binding-induced expansion" mechanism in both TRiC and GroEL, but that binding to TRiC, in addition, causes a large and specific separation of two subdomains in the ß-actin molecule, leading to a distinct expansion of its ATP-binding cleft. Moreover, the binding of ATP and GroES has less effect on the GroEL-bound ß-actin molecule than the ATP binding to TRiC, where it leads to a major compaction of the ß-actin molecule. It can be concluded that the specific and directed rearrangement of the ß-actin structure, seen in the natural ß-actin-TRiC system, is vital for guiding ß-actin to the native state. © 2007 American Chemical Society.
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