NDLI: Selective observation of the disordered import signal of a globular protein by in-cell NMR: the example of frataxins.

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Selective observation of the disordered import signal of a globular protein by in-cell NMR: the example of frataxins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Temussi, Piero Andrea Pastore, Annalisa Popovic, Matija Sanfelice, Domenico Pastore, Chiara Prischi, Filippo
Description	Country affiliation: United kingdom Author Affiliation: Popovic M ( National Institute for Medical Research, MRC, The Ridgeway, London, United Kingdom.); Sanfelice D ( Department of Clinical Neuroscience, King's College London, Denmark Hill Campus, London, United Kingdom.); Pastore C ( Department of Life Sciences, Centre for Structural Biology, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.); Prischi F ( Department of Life Sciences, Centre for Structural Biology, Sir Ernst Chain Building, Imperial College London, London, SW7 2AZ, United Kingdom.); Temussi PA ( National Institute for Medical Research, MRC, The Ridgeway, London, United Kingdom.); Pastore A ( Department of Clinical Neuroscience, King's College London, Denmark Hill Campus, London, United Kingdom.)
Abstract	We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of the bacterial ortholog CyaY cannot be observed in the homologous E. coli system, although it becomes fully observable as soon as the cells are lysed. This behavior has been observed for several other compact globular proteins as seems to be the rule rather than the exception. The NMR spectrum of the yeast ortholog Yfh1 contains instead visible signals from the protein. We demonstrate that they correspond to the flexible N-terminal tail indicating that this is flexible and unfolded. This flexibility of the N-terminus agrees with previous studies of human frataxin, despite the extensive sequence diversity of this region in the two proteins. Interestingly, the residues that we observe in in-cell experiments are not visible in the crystal structure of a Yfh1 mutant designed to destabilize the first helix. More importantly, our results show that, in cell, the protein is predominantly present not as an aggregate but as a monomeric species.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.2679
Journal	Protein Science
Issue Number	6
Volume Number	24
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2015-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Intrinsically Disordered Proteins Chemistry Metabolism Iron-binding Proteins Magnetic Resonance Spectroscopy Cytological Techniques Escherichia Coli Proteins Pliability Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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