Details
| Original language | English |
|---|---|
| Pages (from-to) | 6866-6873 |
| Number of pages | 8 |
| Journal | Angewandte Chemie |
| Volume | 59 |
| Issue number | 17 |
| Early online date | 5 Feb 2020 |
| Publication status | Published - 9 Apr 2020 |
Abstract
Solid-state NMR (ssNMR) is applicable to high molecular-weight (MW) protein assemblies in a non-amorphous precipitate. The technique yields atomic resolution structural information on both soluble and insoluble particles without limitations of MW or requirement of crystals. Herein, we propose and demonstrate an approach that yields the structure of protein–RNA complexes (RNP) solely from ssNMR data. Instead of using low-sensitivity magnetization transfer steps between heteronuclei of the protein and the RNA, we measure paramagnetic relaxation enhancement effects elicited on the RNA by a paramagnetic tag coupled to the protein. We demonstrate that this data, together with chemical-shift-perturbation data, yields an accurate structure of an RNP complex, starting from the bound structures of its components. The possibility of characterizing protein–RNA interactions by ssNMR may enable applications to large RNP complexes, whose structures are not accessible by other methods.
Keywords
- paramagnetic relaxation enhancement, protein–RNA complex, RNA recognition, solid-state NMR, structure determination
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- General Chemistry
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In: Angewandte Chemie , Vol. 59, No. 17, 09.04.2020, p. 6866-6873.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Structure of a Protein–RNA Complex by Solid-State NMR Spectroscopy
AU - Ahmed, Mumdooh
AU - Marchanka, Alexander
AU - Carlomagno, Teresa
N1 - Funding Information: M.A. was supported by the DFG grant CA294/10-1 to T.C.
PY - 2020/4/9
Y1 - 2020/4/9
N2 - Solid-state NMR (ssNMR) is applicable to high molecular-weight (MW) protein assemblies in a non-amorphous precipitate. The technique yields atomic resolution structural information on both soluble and insoluble particles without limitations of MW or requirement of crystals. Herein, we propose and demonstrate an approach that yields the structure of protein–RNA complexes (RNP) solely from ssNMR data. Instead of using low-sensitivity magnetization transfer steps between heteronuclei of the protein and the RNA, we measure paramagnetic relaxation enhancement effects elicited on the RNA by a paramagnetic tag coupled to the protein. We demonstrate that this data, together with chemical-shift-perturbation data, yields an accurate structure of an RNP complex, starting from the bound structures of its components. The possibility of characterizing protein–RNA interactions by ssNMR may enable applications to large RNP complexes, whose structures are not accessible by other methods.
AB - Solid-state NMR (ssNMR) is applicable to high molecular-weight (MW) protein assemblies in a non-amorphous precipitate. The technique yields atomic resolution structural information on both soluble and insoluble particles without limitations of MW or requirement of crystals. Herein, we propose and demonstrate an approach that yields the structure of protein–RNA complexes (RNP) solely from ssNMR data. Instead of using low-sensitivity magnetization transfer steps between heteronuclei of the protein and the RNA, we measure paramagnetic relaxation enhancement effects elicited on the RNA by a paramagnetic tag coupled to the protein. We demonstrate that this data, together with chemical-shift-perturbation data, yields an accurate structure of an RNP complex, starting from the bound structures of its components. The possibility of characterizing protein–RNA interactions by ssNMR may enable applications to large RNP complexes, whose structures are not accessible by other methods.
KW - paramagnetic relaxation enhancement
KW - protein–RNA complex
KW - RNA recognition
KW - solid-state NMR
KW - structure determination
UR - http://www.scopus.com/inward/record.url?scp=85080107363&partnerID=8YFLogxK
U2 - 10.1002/anie.201915465
DO - 10.1002/anie.201915465
M3 - Article
C2 - 32023357
AN - SCOPUS:85080107363
VL - 59
SP - 6866
EP - 6873
JO - Angewandte Chemie
JF - Angewandte Chemie
SN - 1433-7851
IS - 17
ER -