Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy

Subhabrata Majumder; Jing Xue; Christopher M. Demott; Sergey Reverdatto; David S. Burz; Alexander Shekhtman

doi:10.1021/acs.biochem.5b00036

Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy

Subhabrata Majumder, Jing Xue, Christopher M. Demott, Sergey Reverdatto, David S. Burz, Alexander Shekhtman

Research output: Contribution to journal › Article › peer-review

78 Scopus citations

Abstract

Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, weak protein (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro. Cross-correlated relaxation-induced polarization transfer-based in-cell nuclear magnetic resonance allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eukaryotic cells. We show that RNAs are an important component of protein quinary interactions. Protein quinary interactions are unique to the target protein and may affect physicochemical properties, protein activity, and interactions with drugs.

Original language	English (US)
Pages (from-to)	2727-2738
Number of pages	12
Journal	Biochemistry
Volume	54
Issue number	17
DOIs	https://doi.org/10.1021/acs.biochem.5b00036
State	Published - May 5 2015
Externally published	Yes

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© 2015 American Chemical Society.

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AU - Xue, Jing

AU - Demott, Christopher M.

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AU - Burz, David S.

AU - Shekhtman, Alexander

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AB - Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, weak protein (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro. Cross-correlated relaxation-induced polarization transfer-based in-cell nuclear magnetic resonance allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eukaryotic cells. We show that RNAs are an important component of protein quinary interactions. Protein quinary interactions are unique to the target protein and may affect physicochemical properties, protein activity, and interactions with drugs.

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Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy

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