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Literature DB >> 25894651

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

Subhabrata Majumder¹, Jing Xue¹, Christopher M DeMott¹, Sergey Reverdatto¹, David S Burz¹, Alexander Shekhtman¹.

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.

Entities: CellLine Chemical Disease Gene Species

Mesh：

Substances：
DNA Probes
Proteins
RNA

Year: 2015 PMID： 25894651 PMCID： PMC4447238 DOI： 10.1021/acs.biochem.5b00036

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

54 in total

1. Protein-protein interactions: Interactome under construction.

Authors: Laura Bonetta
Journal: Nature Date: 2010-12-09 Impact factor: 49.962

2. Intrinsic motions along an enzymatic reaction trajectory.

Authors: Katherine A Henzler-Wildman; Vu Thai; Ming Lei; Maria Ott; Magnus Wolf-Watz; Tim Fenn; Ed Pozharski; Mark A Wilson; Gregory A Petsko; Martin Karplus; Christian G Hübner; Dorothee Kern
Journal: Nature Date: 2007-11-18 Impact factor: 49.962

3. Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes.

Authors: Philipp Selenko; Zach Serber; Bedrick Gadea; Joan Ruderman; Gerhard Wagner
Journal: Proc Natl Acad Sci U S A Date: 2006-07-27 Impact factor: 11.205

4. The STINT-NMR method for studying in-cell protein-protein interactions.

Authors: David S Burz; Alexander Shekhtman
Journal: Curr Protoc Protein Sci Date: 2010-08

5. Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O.

Authors: Shinji Ogino; Satoshi Kubo; Ryo Umemoto; Shuxian Huang; Noritaka Nishida; Ichio Shimada
Journal: J Am Chem Soc Date: 2009-08-12 Impact factor: 15.419

6. Protein (19)F NMR in Escherichia coli.

Authors: Conggang Li; Gui-Fang Wang; Yaqiang Wang; Rachel Creager-Allen; Evan A Lutz; Heidi Scronce; Kristin M Slade; Rebecca A S Ruf; Ryan A Mehl; Gary J Pielak
Journal: J Am Chem Soc Date: 2010-01-13 Impact factor: 15.419

7. Effects of macromolecular crowding on protein conformational changes.

Authors: Hao Dong; Sanbo Qin; Huan-Xiang Zhou
Journal: PLoS Comput Biol Date: 2010-07-01 Impact factor: 4.475

8. Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR).

Authors: Jingjing Xie; Rajiv Thapa; Sergey Reverdatto; David S Burz; Alexander Shekhtman
Journal: J Med Chem Date: 2009-06-11 Impact factor: 7.446

9. High-resolution multi-dimensional NMR spectroscopy of proteins in human cells.

Authors: Kohsuke Inomata; Ayako Ohno; Hidehito Tochio; Shin Isogai; Takeshi Tenno; Ikuhiko Nakase; Toshihide Takeuchi; Shiroh Futaki; Yutaka Ito; Hidekazu Hiroaki; Masahiro Shirakawa
Journal: Nature Date: 2009-03-05 Impact factor: 49.962

10. Protein structure determination in living cells by in-cell NMR spectroscopy.

Authors: Daisuke Sakakibara; Atsuko Sasaki; Teppei Ikeya; Junpei Hamatsu; Tomomi Hanashima; Masaki Mishima; Masatoshi Yoshimasu; Nobuhiro Hayashi; Tsutomu Mikawa; Markus Wälchli; Brian O Smith; Masahiro Shirakawa; Peter Güntert; Yutaka Ito
Journal: Nature Date: 2009-03-05 Impact factor: 49.962

29 in total

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

1. Protein-protein interactions: Interactome under construction.

2. Intrinsic motions along an enzymatic reaction trajectory.

3. Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes.

4. The STINT-NMR method for studying in-cell protein-protein interactions.

5. Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O.

6. Protein (19)F NMR in Escherichia coli.

7. Effects of macromolecular crowding on protein conformational changes.

8. Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR).

9. High-resolution multi-dimensional NMR spectroscopy of proteins in human cells.

10. Protein structure determination in living cells by in-cell NMR spectroscopy.

1. Ribosome Mediated Quinary Interactions Modulate In-Cell Protein Activities.

Review 2. A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.

3. Quinary interactions with an unfolded state ensemble.

Review 4. Interaction proteomics by using in-cell NMR spectroscopy.

Review 5. New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.

6. Improved sensitivity and resolution of in-cell NMR spectra.

Review 7. In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.

8. Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.

9. Intracellular pH modulates quinary structure.

10. Total Cellular RNA Modulates Protein Activity.