Back to Search
Start Over
Tubulin folding: the special case of a beta-tubulin isotype from the Antarctic psychrophilic ciliate Euplotes focardii
- Source :
- Polar Biology, Polar Biology, Springer Verlag, 2013, 36 (12), pp.1833-1838. ⟨10.1007/s00300-013-1390-9⟩, Polar biology, 36 (2013): 1833–1838. doi:10.1007/s00300-013-1390-9, info:cnr-pdr/source/autori:Pucciarelli, Sandra; Chiappori, Federica; Sparvoli, Daniela; Milanesi, Luciano; Miceli, Cristina; Melki, Ronald/titolo:Tubulin folding: the special case of a beta-tubulin isotype from the Antarctic psychrophilic ciliate Euplotes focardii/doi:10.1007%2Fs00300-013-1390-9/rivista:Polar biology (Print)/anno:2013/pagina_da:1833/pagina_a:1838/intervallo_pagine:1833–1838/volume:36
- Publication Year :
- 2013
- Publisher :
- Springer Science and Business Media LLC, 2013.
-
Abstract
- International audience; Folding assistance is a fundamental requirement of certain proteins, and it may be subjected to physicochemical constraints in case of organisms adapted to polar temperatures. Limited information is available about protein folding in the polar environment. Folding of tubulin provides one of the few studied cases. Here, we report a pilot folding analysis of a divergent beta-tubulin isotype, named EFBT3, from the Antarctic psychrophilic ciliate Euplotes focardii. To attain its native monomeric structure, beta-tubulin needs the assistance of the eukaryotic class II chaperonin CCT and cofactor A (CofA). The in vitro folding reaction of EFBT3 with CCT and CofA purified from rabbit did not generate any folded product. In contrast, the reaction performed with the rabbit reticulocyte lysate, that contains all the chaperones required for efficient tubulin folding, was productive, suggesting that additional factors besides purified CCT and CofA are required for EFBT3 to attain its monomeric structure. We also demonstrated that the rare Cys281 of EFBT3 is critical for the folding reaction. Model predictions indicate that EFBT3 binds to CofA differently from yeast beta-tubulin, suggesting a diverse folding mechanism that may be correlated with microtubule cold adaptation.
- Subjects :
- [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
macromolecular substances
Sitedirected mutagenesis
03 medical and health sciences
0302 clinical medicine
Reticulocyte
Microtubule
medicine
Psychrophile
Site-directed mutagenesis
030304 developmental biology
Molecular chaperons
0303 health sciences
[SDV.NEU.PC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior
biology
Cold adaptation
Modeling
[SDV.NEU.SC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Cognitive Sciences
Tubulin cofactor A
Yeast
Folding (chemistry)
Tubulin
medicine.anatomical_structure
Biochemistry
Protozoan
biology.protein
Protein folding
General Agricultural and Biological Sciences
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 14322056 and 07224060
- Volume :
- 36
- Database :
- OpenAIRE
- Journal :
- Polar Biology
- Accession number :
- edsair.doi.dedup.....60197804777dfb9a72795ac46ef58aaa